| Superfamily | Description | Comments |
|---|
| a.1.1 | Globin-like | core: 6 helices; folded leaf, partly opened |
| a.3.1 | Cytochrome c | core: 3 helices; folded leaf, opened |
| a.4.1 | DNA/RNA-binding 3-helical bundle | core: 3-helices; bundle, closed or partly opened, right-handed twist; up-and down |
| a.4.5 | DNA/RNA-binding 3-helical bundle | core: 3-helices; bundle, closed or partly opened, right-handed twist; up-and down |
| a.4.6 | DNA/RNA-binding 3-helical bundle | core: 3-helices; bundle, closed or partly opened, right-handed twist; up-and down |
| a.5.2 | RuvA C-terminal domain-like | 3 helices; bundle, right-handed twist |
| a.6.1 | Putative DNA-binding domain | core: 3 helices; architecture is similar to that of the "winged helix" fold but topology is different |
| a.16.1 | S15/NS1 RNA-binding domain | 3 helices; irregular array |
| a.22.1 | Histone-fold | core: 3 helices; long middle helix is flanked at each end with shorter ones |
| a.25.1 | Ferritin-like | core: 4 helices; bundle, closed, left-handed twist; 1 crossover connection |
| a.26.1 | 4-helical cytokines | core: 4 helices; bundle, closed; left-handed twist; 2 crossover connections |
| a.35.1 | lambda repressor-like DNA-binding domains | core: 4 helices; folded leaf, closed |
| a.39.1 | EF Hand-like | core: 4 helices; array of 2 hairpins, opened |
| a.43.1 | Ribbon-helix-helix | core: 4 helices; array of 2 hairpins, opened |
| a.52.1 | Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin | 4 helices; folded leaf; right-handed superhelix |
| a.60.1 | SAM domain-like | 4-5 helices; bundle of two orthogonally packed alpha-hairpins; involved in the interactions with DNA and proteins |
| a.74.1 | Cyclin-like | core: 5 helices; one helix is surrounded by the others |
| a.77.1 | DEATH domain | 6 helices: closed bundle; greek-key; internal pseudo twofold symmetry |
| a.93.1 | Heme-dependent peroxidases | multihelical; consists of two all-alpha domains |
| a.100.1 | 6-phosphogluconate dehydrogenase C-terminal domain-like | multihelical; common core is formed around two long antiparallel helices related by (pseudo) twofold symmetry |
| a.102.4 | alpha/alpha toroid | multihelical; up to seven alpha-hairpins are arranged in closed circular array; there may be sequence similarities between different superfamilies |
| a.118.1 | alpha-alpha superhelix | multihelical; 2 (curved) layers: alpha/alpha; right-handed superhelix |
| a.129.1 | GroEL equatorial domain-like | multihelical; 8 helices arranged in 2 parallel layers |
| a.132.1 | Heme oxygenase-like | multihelical; bundle |
| a.138.1 | Multiheme cytochromes | variable number of helices and little beta structure; not a true fold |
| b.1.1 | Immunoglobulin-like beta-sandwich | sandwich; 7 strands in 2 sheets; greek-key ! some members of the fold have additional strands |
| b.1.18 | Immunoglobulin-like beta-sandwich | sandwich; 7 strands in 2 sheets; greek-key ! some members of the fold have additional strands |
| b.1.11 | Immunoglobulin-like beta-sandwich | sandwich; 7 strands in 2 sheets; greek-key ! some members of the fold have additional strands |
| b.2.2 | Common fold of diphtheria toxin/transcription factors/cytochrome f | sandwich; 9 strands in 2 sheet; greek-key; subclass of immunoglobin-like fold |
| b.2.3 | Common fold of diphtheria toxin/transcription factors/cytochrome f | sandwich; 9 strands in 2 sheet; greek-key; subclass of immunoglobin-like fold |
| b.2.5 | Common fold of diphtheria toxin/transcription factors/cytochrome f | sandwich; 9 strands in 2 sheet; greek-key; subclass of immunoglobin-like fold |
| b.6.1 | Cupredoxin-like | sandwich; 7 strands in 2 sheets, greek-key ! variations: some members have additional 1-2 strands |
| b.7.1 | C2 domain-like | sandwich; 8 strands in 2 sheets; greek-key |
| b.121.4 | Nucleoplasmin-like/VP (viral coat and capsid proteins) | sandwich; 8 strands in 2 sheets; jelly-roll; some members can have additional 1-2 strands ! characteristic interaction between the domains of this fold allows the formation of five-fold and pseudo six-fold assemblies |
| b.121.5 | Nucleoplasmin-like/VP (viral coat and capsid proteins) | sandwich; 8 strands in 2 sheets; jelly-roll; some members can have additional 1-2 strands ! characteristic interaction between the domains of this fold allows the formation of five-fold and pseudo six-fold assemblies |
| b.12.1 | Lipase/lipooxygenase domain (PLAT/LH2 domain) | sandwich; 8 strands in 2 sheets; complex topology ! duplication: has weak internal pseudo twofold symmetry |
| b.18.1 | Galactose-binding domain-like | sandwich; 9 strands in 2 sheets; jelly-roll |
| b.19.1 | Viral protein domain | sandwich; 9 strands in 2 sheets; jelly-roll; form trimers |
| b.26.1 | SMAD/FHA domain | sandwich; 11 strands in 2 sheets; greek-key |
| b.29.1 | Concanavalin A-like lectins/glucanases | sandwich; 12-14 strands in 2 sheets; complex topology |
| b.30.5 | Supersandwich | sandwich; 18 strands in 2 sheets |
| b.34.9 | SH3-like barrel | barrel, partly opened; n*=4, S*=8; meander ! the last strand is interrupted by a turn of 3-10 helix |
| b.35.1 | GroES-like | contains barrel, partly opened; n*=4, S*=8; meander |
| b.36.1 | PDZ domain-like | contains barrel, partly opened; n*=4, S*=8; meander; capped by alpha-helix |
| b.40.2 | OB-fold | barrel, closed or partly opened n=5, S=10 or S=8; greek-key |
| b.40.4 | OB-fold | barrel, closed or partly opened n=5, S=10 or S=8; greek-key |
| b.40.6 | OB-fold | barrel, closed or partly opened n=5, S=10 or S=8; greek-key |
| b.42.1 | beta-Trefoil | barrel, closed; n=6, S=12; and a hairpin triplet; meander ! duplication: has internal pseudo threefold symmetry |
| b.42.4 | beta-Trefoil | barrel, closed; n=6, S=12; and a hairpin triplet; meander ! duplication: has internal pseudo threefold symmetry |
| b.43.4 | Reductase/isomerase/elongation factor common domain | barrel, closed; n=6, S=10; greek-key |
| b.45.1 | FMN-binding split barrel | barrel; n=6, S=10; greek-key |
| b.47.1 | Trypsin-like serine proteases | barrel, closed; n=6, S=8; greek-key ! duplication: consists of two domains of the same fold |
| b.49.2 | Domain of alpha and beta subunits of F1 ATP synthase-like | barrel, closed; n=6, S=8; greek-key |
| b.50.1 | Acid proteases | barrel, closed; n=6, S=10, complex topology |
| b.52.2 | Double psi beta-barrel | barrel, closed; n=6, S=10; complex topology with crossover (psi) loops |
| b.55.1 | PH domain-like | barrel, partly opened; n*=6, S*=12; meander; capped by an alpha-helix |
| b.60.1 | Lipocalins | barrel, closed or opened; n=8, S=12; meander |
| b.71.1 | Glycosyl hydrolase domain | folded sheet; greek-key |
| b.80.1 | Single-stranded right-handed beta-helix | superhelix turns are made of parallel beta-strands and (short) turns |
| b.81.1 | Single-stranded left-handed beta-helix | superhelix turns are made of parallel beta-strands and (short) turns |
| b.82.1 | Double-stranded beta-helix | one turn of helix is made by two pairs of antiparallel strands linked with short turns ! has appearance of a sandwich of distinct architecture and jelly-roll topology |
| b.84.2 | Barrel-sandwich hybrid | sandwich of half-barrel shaped beta-sheets |
| b.92.1 | Composite domain of metallo-dependent hydrolases | pseudobarrel; mixed sheet of 7 strand folded upon itself and "buckled" by two beta-turns |
| b.122.1 | PUA domain-like | pseudobarrel; mixed folded sheet of 5 strands; order 13452; strand 1 and 3 are parallel to each other |
| c.1.2 | TIM beta/alpha-barrel | contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 ! the first seven superfamilies have similar phosphate-binding sites |
| c.1.8 | TIM beta/alpha-barrel | contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 ! the first seven superfamilies have similar phosphate-binding sites |
| c.1.9 | TIM beta/alpha-barrel | contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 ! the first seven superfamilies have similar phosphate-binding sites |
| c.1.10 | TIM beta/alpha-barrel | contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 ! the first seven superfamilies have similar phosphate-binding sites |
| c.1.11 | TIM beta/alpha-barrel | contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 ! the first seven superfamilies have similar phosphate-binding sites |
| c.1.12 | TIM beta/alpha-barrel | contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 ! the first seven superfamilies have similar phosphate-binding sites |
| c.2.1 | NAD(P)-binding Rossmann-fold domains | core: 3 layers, a/b/a; parallel beta-sheet of 6 strands, order 321456 ! The nucleotide-binding modes of this and the next two folds/superfamilies are similar |
| c.3.1 | FAD/NAD(P)-binding domain | core: 3 layers, b/b/a; central parallel beta-sheet of 5 strands, order 32145; top antiparallel beta-sheet of 3 strands, meander |
| c.8.5 | The "swivelling" beta/beta/alpha domain | 3 layers: b/b/a; the central sheet is parallel, and the other one is antiparallel; there are some variations in topology ! this domain is thought to be mobile in most multi-domain proteins known to contain it |
| c.10.2 | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | 2 curved layers, a/b; parallel beta-sheet; order 1234...N; there are sequence similarities between different superfamilies |
| c.14.1 | ClpP/crotonase | core: 4 turns of (beta-beta-alpha)n superhelix |
| c.18.1 | DNA glycosylase | 3 layers, a/b/a; core: parallel beta-sheet of 4 strands, order 2134 |
| c.58.1 | Aminoacid dehydrogenase-like, N-terminal domain | core: 3 layers: a/b/a; parallel beta-sheet of 4 strands; 2134 |
| c.23.5 | Flavodoxin-like | 3 layers, a/b/a; parallel beta-sheet of 5 strand, order 21345 |
| c.23.16 | Flavodoxin-like | 3 layers, a/b/a; parallel beta-sheet of 5 strand, order 21345 |
| c.25.1 | Ferredoxin reductase-like, C-terminal NADP-linked domain | 3 layers, a/b/a; parallel beta-sheet of 5 strands, order 32145 |
| c.26.1 | Adenine nucleotide alpha hydrolase-like | core: 3 layers, a/b/a ; parallel beta-sheet of 5 strands, order 32145 |
| c.26.2 | Adenine nucleotide alpha hydrolase-like | core: 3 layers, a/b/a ; parallel beta-sheet of 5 strands, order 32145 |
| c.116.1 | alpha/beta knot | core: 3 layers: a/b/a, parallel beta-sheet of 5 strands, order 21435; contains a deep trefoil knot |
| c.30.1 | PreATP-grasp domain | 3 layers: a/b/a; parallel or mixed beta-sheet of 4 to 6 strands ! possible rudiment form of Rossmann-fold domain |
| c.31.1 | DHS-like NAD/FAD-binding domain | 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 321456; Rossmann-like |
| c.124.1 | NagB/RpiA/CoA transferase-like | core: 3 layers: a/b/a; parallel or mixed beta-sheet of 6 strands, order 321456 |
| c.36.1 | Thiamin diphosphate-binding fold (THDP-binding) | 3 layers: a/b/a; parallel beta-sheet of 6 strands, order 213465 |
| c.37.1 | P-loop containing nucleoside triphosphate hydrolases | 3 layers: a/b/a, parallel or mixed beta-sheets of variable sizes |
| c.41.1 | Subtilisin-like | 3 layers: a/b/a, parallel beta-sheet of 7 strands, order 2314567; left-handed crossover connection between strands 2 & 3 |
| c.43.1 | CoA-dependent acyltransferases | core: 2 layers, a/b; mixed beta-sheet of 6 strands, order 324561; strands 3 & 6 are antiparallel to the rest |
| c.45.1 | (Phosphotyrosine protein) phosphatases II | core: 3 layers, a/b/a; parallel beta-sheet of 4 strands, order 1423 |
| c.46.1 | Rhodanese/Cell cycle control phosphatase | 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 32451 |
| c.47.1 | Thioredoxin fold | core: 3 layers, a/b/a; mixed beta-sheet of 4 strands, order 4312; strand 3 is antiparallel to the rest |
| c.48.1 | TK C-terminal domain-like | 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 13245, strand 1 is antiparallel to the rest |
| c.55.1 | Ribonuclease H-like motif | 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32145; strand 2 is antiparallel to the rest |
| c.55.3 | Ribonuclease H-like motif | 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32145; strand 2 is antiparallel to the rest |
| c.56.5 | Phosphorylase/hydrolase-like | core: 3 layers, a/b/a ; mixed sheet of 5 strands: order 21354; strand 4 is antiparallel to the rest; contains crossover loops |
| c.57.1 | Molybdenum cofactor biosynthesis proteins | 3 layers: a/b/a; mixed beta-sheet of 5 strands; order: 21354, strand 5 is antiparallel to the rest; permutation of the Phosphorylase/hydrolase-like fold |
| c.60.1 | Phosphoglycerate mutase-like | core: 3 layers, a/b/a; mixed beta-sheet of 6 strands, order 324156; strand 5 is antiparallel to the rest |
| c.66.1 | S-adenosyl-L-methionine-dependent methyltransferases | core: 3 layers, a/b/a; mixed beta-sheet of 7 strands, order 3214576; strand 7 is antiparallel to the rest |
| c.67.1 | PLP-dependent transferases | main domain: 3 layers: a/b/a, mixed beta-sheet of 7 strands, order 3245671; strand 7 is antiparallel to the rest |
| c.68.1 | Nucleotide-diphospho-sugar transferases | 3 layers: a/b/a; mixed beta-sheet of 7 strands, order 3214657; strand 6 is antiparallel to the rest |
| c.69.1 | alpha/beta-Hydrolases | core: 3 layers, a/b/a; mixed beta-sheet of 8 strands, order 12435678, strand 2 is antiparallel to the rest |
| c.72.1 | Ribokinase-like | core: 3 layers: a/b/a; mixed beta-sheet of 8 strands, order 21345678, strand 7 is antiparallel to the rest ! potential superfamily: members of this fold have similar functions but different ATP-binding sites |
| c.76.1 | Alkaline phosphatase-like | core:3 layers: a/b/a; mixed beta-sheet of 8 strands, order 43516728, strand 7 is antiparallel to the rest |
| c.80.1 | SIS domain | 3 layers: a/b/a; parallel beta-sheet of 5 strands, order 21345 |
| c.87.1 | UDP-Glycosyltransferase/glycogen phosphorylase | consists of two non-similar domains with 3 layers (a/b/a) each ! domain 1: parallel beta-sheet of 7 strands, order 3214567 ! domain 2: parallel beta-sheet of 6 strands, order 321456 |
| c.91.1 | PEP carboxykinase-like | contains a P-loop NTP-binding motif; mixed beta-sheet folds into a barrel-like structure with helices packed on one side |
| c.92.2 | Chelatase-like | duplication: tandem repeat of two domains; 3 layers (a/b/a); parallel beta-sheet of 4 strands, order 2134 |
| c.94.1 | Periplasmic binding protein-like II | consists of two similar intertwined domain with 3 layers (a/b/a) each: duplication ! mixed beta-sheet of 5 strands, order 21354; strand 5 is antiparallel to the rest |
| c.95.1 | Thiolase-like | consists of two similar domains related by pseudo dyad; duplication ! 3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32451; strand 5 is antiparallel to the rest |
| d.1.1 | Microbial ribonucleases | single helix packs against antiparallel beta-sheet |
| d.2.1 | Lysozyme-like | common alpha+beta motif for the active site region |
| d.3.1 | Cysteine proteinases | consists of one alpha-helix and 4 strands of antiparallel beta-sheet and contains the catalytic triad Cys-His-Asn |
| d.13.1 | HIT-like | alpha-beta(3)-alpha-beta(2); 3 layers: alpha/beta/alpha |
| d.14.1 | Ribosomal protein S5 domain 2-like | core: beta(3)-alpha-beta-alpha; 2 layers: alpha/beta; left-handed crossover |
| d.15.1 | beta-Grasp (ubiquitin-like) | core: beta(2)-alpha-beta(2); mixed beta-sheet 2143 |
| d.15.2 | beta-Grasp (ubiquitin-like) | core: beta(2)-alpha-beta(2); mixed beta-sheet 2143 |
| d.15.3 | beta-Grasp (ubiquitin-like) | core: beta(2)-alpha-beta(2); mixed beta-sheet 2143 |
| d.15.4 | beta-Grasp (ubiquitin-like) | core: beta(2)-alpha-beta(2); mixed beta-sheet 2143 |
| d.16.1 | FAD-linked reductases, C-terminal domain | alpha+beta sandwich |
| d.32.1 | Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase | beta-alpha-beta(3); 2 layers: alpha/beta |
| d.38.1 | Thioesterase/thiol ester dehydrase-isomerase | core: beta-alpha-beta(4); 2 layers: alpha/beta |
| d.42.1 | POZ domain | core: beta(2)-alpha(2)-beta(2)-alpha(2); 2 layers a/b; mixed sheet: 2143 |
| d.218.1 | Nucleotidyltransferase | core: alpha-beta-turn-beta-X-beta-(alpha); mixed beta-sheet, order of core strands: 123 |
| d.56.1 | GroEL-intermediate domain like | 3-helical bundle packed against 3-stranded mixed beta-sheet |
| d.58.1 | Ferredoxin-like | alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2 |
| d.58.3 | Ferredoxin-like | alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2 |
| d.58.4 | Ferredoxin-like | alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2 |
| d.58.5 | Ferredoxin-like | alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2 |
| d.58.7 | Ferredoxin-like | alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2 |
| d.58.31 | Ferredoxin-like | alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2 |
| d.265.1 | Pseudouridine synthase | consists of two alpha+beta subdomains with some similarity to the ferredoxin-like fold |
| d.185.1 | LuxS/MPP-like metallohydrolase | core: beta-alpha-beta(2)-alpha(2); 2 layers: alpha/beta |
| d.79.1 | Bacillus chorismate mutase-like | core: beta-alpha-beta-alpha-beta(2); mixed beta-sheet: order: 1423, strand 4 is antiparallel to the rest |
| d.79.3 | Bacillus chorismate mutase-like | core: beta-alpha-beta-alpha-beta(2); mixed beta-sheet: order: 1423, strand 4 is antiparallel to the rest |
| d.80.1 | Tautomerase/MIF | (beta-alpha-beta)2; 2 layers: alpha/beta; mixed beta-sheet ! generally forms trimers with three closely packed beta-sheets |
| d.81.1 | Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain | core: alpha-beta-alpha-beta(3); mixed sheet: 2134, strand 2 is parallel to strand 1 |
| d.92.1 | Zincin-like | contains mixed beta sheet with connection over free side of the sheet |
| d.95.2 | Homing endonuclease-like | alpha-beta(2)-alpha-beta(2)-alpha; 2 layers: a/b; antiparallel sheet 1243 |
| d.96.1 | T-fold | beta(2)-alpha(2)-beta(2); 2 layers: alpha/beta; antiparallel sheet 1234 ! tunnel-shaped: its known members form wide oligomeric barrels different sizes |
| d.108.1 | Acyl-CoA N-acyltransferases (Nat) | 3 layers: a/b/a; contains mixed beta-sheet |
| d.109.1 | Gelsolin-like | 3 layers: a/b/a; contains mixed beta-sheet |
| d.110.2 | Profilin-like | core: 2 alpha-helices and 5-stranded antiparallel sheet: order 21543; 3 layers: alpha/beta/alpha |
| d.110.3 | Profilin-like | core: 2 alpha-helices and 5-stranded antiparallel sheet: order 21543; 3 layers: alpha/beta/alpha |
| d.113.1 | Nudix | beta(2)-alpha-beta(3)-alpha; 3 layers: alpha/beta/alpha; mixed sheet ! contains beta-grasp motif |
| d.115.1 | YrdC/RibB | core: alpha-beta(2)-alpha-beta-alpha(2)-beta(2)-alpha-beta-alpha-beta; 3 layers; mixed twisted sheet of 7 strands; order 7126354; strands 7 and 1 are parallel to each other |
| d.122.1 | ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase | 8-stranded mixed beta-sheet; 2 layers: alpha/beta |
| d.129.3 | TBP-like | beta-alpha-beta(4)-alpha |
| d.131.1 | DNA clamp | contains two helices and two beta sheets ! duplication: fold has internal pseudo two-fold symmetry |
| d.142.1 | ATP-grasp | Consists of two subdomains with different alpha+beta folds ! shares functional and structural similarities with the PIPK and protein kinase superfamilies |
| d.145.1 | FAD-binding domain | consists of two alpha+beta subdomains |
| d.153.1 | Ntn hydrolase-like | 4 layers: alpha/beta/beta/alpha; has an unusual sheet-to-sheet packing |
| d.159.1 | Metallo-dependent phosphatases | 4 layers: alpha/beta/beta/alpha; mixed beta sheets; contains duplication |
| d.162.1 | LDH C-terminal domain-like | unusual fold, defines family |
| d.163.1 | DNA breaking-rejoining enzymes | core: alpha3-beta3-alpha4; one side of beta-sheet is exposed |
| d.166.1 | ADP-ribosylation | unusual fold |
| d.169.1 | C-type lectin-like | unusual fold |
| e.8.1 | DNA/RNA polymerases | divided into morphological domains including "palm", "thumb" and "fingers"; the catalytic "palm" domain is conserved to all members |
| e.29.1 | beta and beta-prime subunits of DNA dependent RNA-polymerase | Multidomain subunits of complex domain organization |
| f.4.3 | Transmembrane beta-barrels | not a true fold, gathers together transmembrane barrels of different (n,S) |
| g.3.6 | Knottins (small inhibitors, toxins, lectins) | disulfide-bound fold; contains beta-hairpin with two adjacent disulfides |
| g.3.7 | Knottins (small inhibitors, toxins, lectins) | disulfide-bound fold; contains beta-hairpin with two adjacent disulfides |
| g.3.11 | Knottins (small inhibitors, toxins, lectins) | disulfide-bound fold; contains beta-hairpin with two adjacent disulfides |
| g.3.15 | Knottins (small inhibitors, toxins, lectins) | disulfide-bound fold; contains beta-hairpin with two adjacent disulfides |
| g.7.1 | Snake toxin-like | disulfide-rich fold: nearly all-beta |
| g.8.1 | BPTI-like | disulfide-rich alpha+beta fold |
| g.14.1 | Kringle-like | disulfide-rich fold; nearly all-beta |
| g.17.1 | Cystine-knot cytokines | disulfide-rich fold; common core is all-beta |
| g.24.1 | TNF receptor-like | duplication: consists of three similar disulfide-rich domains |
| g.37.1 | C2H2 and C2HC zinc fingers | alpha+beta metal(zinc)-bound fold: beta-hairpin + alpha-helix |
| g.39.1 | Glucocorticoid receptor-like (DNA-binding domain) | alpha+beta metal(zinc)-bound fold |
| g.41.5 | Rubredoxin-like | metal(zinc or iron)-bound fold; sequence contains two CX(n)C motifs, in most cases n = 2 |
| g.50.1 | FYVE/PHD zinc finger | dimetal(zinc)-bound alpha+beta fold |