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proteins containing predominantly beta-strands

Derived from SCOP 48724

## Class

class All beta proteins (1000001)proteins containing predominantly beta-strands

Derived from SCOP 48724

## Children

- fold GroES-like (2000001)

contains barrel, partly opened, n*=4, S*=8, meander

Derived from SCOP 50128 - fold Supersandwich (2000003)

sandwich, 18 strands in 2 sheets

Derived from SCOP 49993 - fold EF/AMT-type beta(6)-barrel (2000004)

barrel, closed, n=6, S=10, greek-key; antiparallel sheet, clockwise order: 143256

Derived from SCOP 50464 - fold FMT/AAG-type beta(6)-barrel (2000011)

barrel, open, n*=6, S*=10, greek-key; antiparallel beta-sheet, clockwise order: 125436

Derived from SCOP 50485 - fold HI0933-type beta(6)-barrel (2000028)

barrel, closed, n=6, S=12, greek-key; clockwise order: 143256

Derived from SCOP 160995 - fold TNF-like (2000041)

sandwich, 10 strands in 2 sheets, jelly-roll

Derived from SCOP 49841 - fold Double-stranded beta-helix (2000048)

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

Derived from SCOP 51181 - fold Immunoglobulin-like beta-sandwich (2000051)

sandwich, 7 strands in 2 sheets, greek-key some members of the fold have additional strands

Derived from SCOP 48725 - fold Mu transposase-type beta(6)-barrel (2000126)

barrel; n=6, S=8, greek-key; antiparallel beta-sheet, clockwise order: 145632

Derived from SCOP 50609 - fold Fpg N-terminal domain-like (2000055)

pseudobarrel, capped on both ends by alpha-helices

Derived from SCOP 81625 - fold Single-stranded right-handed beta-helix (2000062)

superhelix turns are made of parallel beta-strands and (short) turns

Derived from SCOP 51125 - fold Galactose-binding domain-like (2000064)

sandwich, 9 strands in 2 sheets, jelly-roll

Derived from SCOP 49784 - fold RIFT-type beta(6)-barrel (2000073)

barrel, closed, n=6, S=10, greek-key; antiparallel beta-sheet, order 125436 (anticlockwise)

Derived from SCOP 50412 - fold Trypsin-type beta(6)-barrel (2000083)

barrel, closed, n=6, S=8, greek-key; antiparallel beta-sheet, order: 123654 (clockwise)

Derived from SCOP 50493 - fold Concanavalin-like (2000089)

sandwich, 12-14 strands in 2 sheets, complex topology

Derived from SCOP 49898 - fold SH3-like barrel (2000090)

barrel, partly opened, n*=4, S*=8, meander the last strand is interrupted by a turn of 3-10 helix

Derived from SCOP 50036 - fold OB-fold (2000100)

beta(5)-barrel, closed or partly opened n=5, S=10 or S=8, greek-key; mixed beta-sheet, order 12354 (anticlockwise), strands 3 and 5 are parallel to each other

Derived from SCOP 50198 - fold PH domain-like beta(6)-barrel (2000118)

barrel, partly opened; n*=6, S*=12; meander; capped by the C-terminal alpha-helix

Derived from SCOP 50728 - fold SMAD/FHA domain-like (2000121)

sandwich; 11 strands in 2 sheets; greek-key

Derived from SCOP 49878 - fold RAP-type triple barrel (2000124)

heterodimer of two related subunits; forms two similar barrels, n=8, S=10 each, which are fused together with the formation of a third barrel, n=6, S=8

Derived from SCOP 50915 - fold beta-clip (2000138)

double-stranded ribbon sharply bent in two places; the ribbon ends form incomplete barrel; jelly-roll

Derived from SCOP 51268 - fold ZU5 domain-like (2000140)

core: beta-sandwich, 8 strands in 2 sheets; folded meander - fold CsrA-like (2000231)

sandwich, 10 strands in 2 sheets, intertwined dimer (segment-swapped, 5-stranded greek-key sandwich?)

Derived from SCOP 117129 - fold PDZ domain-like (2000296)

contains barrel, partly opened, n*=4, S*=8, meander, capped by alpha-helix

Derived from SCOP 50155 - fold PUA domain-like (2000644)

pseudobarrel, mixed folded sheet of 5 strands, order 13452, strand 1 and 3 are parallel to each other

Derived from SCOP 88696 - fold ATP synthase beta-barrel domain-like (2000654)

barrel, closed, n=6, S=8, greek-key

Derived from SCOP 50614 - fold hsp20-like chaperones (2000764)

sandwich, 8 strands in 2 sheets, greek-key

Derived from SCOP 49763 - fold Obg-fold (2000882)

this fold is formed by three glycine-rich regions inserted into a small 8-stranded beta-sandwich these regions form six left-handed collagen-like helices packed and H-bonded together

Derived from SCOP 82050 - fold MalF P2 barrel-like (2001003)

beta-barrel (n=7, S=8); mixed, mostly antiparallel beta-sheet, order 1234567; overside loop between the parallel strands 4 and 5

Derived from SCOP 160963 - fold Barrel-sandwich hybrid (2001151)

sandwich of half-barrel shaped beta-sheets

Derived from SCOP 51229 - iupr Extended binder (2000139)

binds to a globular domain in an extended conformation with the formation of short beta-strand(s)