Structural Tag

mixed beta-sheet (15)

At least one strand is parallel to one of its two neighbours and antiparallel to the other.

Nodes

  • fold Formyltransferase-type (2000023)
    3 layers: a/b/a, mixed beta-sheet of 7 strands, order 3214567, strand 6 is antiparallel to the rest
    Derived from SCOP 53327
  • fold Thioredoxin fold (2000024)
    core: 3 layers, a/b/a, mixed beta-sheet of 4 strands, order: 2134, strand 3 is antiparallel to the rest
    Derived from SCOP 52832
  • fold Canonical FwdE/GAPDH domain-like fold (2000032)
    alpha-beta-alpha-beta(3), 2 layers, alpha/beta sandwich, mixed sheet: 2134, strand 2 is parallel to strand 1, psi-loop between strands 2 and 3
    Derived from SCOP 55346
  • fold Class II aaRS/BPL domain-like (2000038)
    core: beta-X-beta(2)-alpha-beta(4); mixed, mostly antiparallel beta-sheet, order 1237654, strands 1 and 2 are parallel to each other
    Derived from SCOP 55680
  • fold PRTase-like (2000040)
    3 layers, a/b/a, mixed beta-sheet of 6 strands, order 321456, strand 3 is antiparallel to the rest
    Derived from SCOP 53270
  • fold Resolvase-like (2000045)
    Core: 3 layers: a/b/a, mixed beta-sheet of 5 strands, order 21345, strand 5 is antiparallel to the rest
    Derived from SCOP 53040
  • fold NDP Glycotransferase-like (2000056)
    3 layers: a/b/a, mixed beta-sheet of 7 strands, order 3214657, strand 6 is antiparallel to the rest
    Derived from SCOP 53447
  • fold FPGS-type ribokinase-like fold (2000058)
    core: 3 layers: a/b/a, mixed beta-sheet of 8 strands, order 21345678, strand 7 is antiparallel to the rest
    Derived from SCOP 53612
  • fold GHKL domain-like (2000066)
    2 layers: alpha/beta; 8-stranded mixed beta-sheet, order: 87126345, strands 1 and 7 are parallel to each other
    Derived from SCOP 55873
  • fold alpha/beta-Hydrolases (2000076)
    core: 3 layers, a/b/a, mixed beta-sheet of 8 strands, order 12435678, strand 2 is antiparallel to the rest
    Derived from SCOP 53473
  • fold Restriction endonuclease-like (2000077)
    alpha-beta(3)-alpha-beta; 3 layers, a/b/a, mixed beta-sheet, order: 1234, strands 2 is antiparallel to the rest
    Derived from SCOP 52979
  • fold FPGS C-terminal domain-like (2000079)
    3 layers: a/b/a, mixed beta-sheet of 6 strands, order 126345, strand 1 is antiparallel to the rest
    Derived from SCOP 53243
  • fold MoeB-like (2000082)
    3 layers: a/b/a, mixed beta-sheet of 8 strands, order 32145678, strands 6 and 8 are antiparallel to the rest
    Derived from SCOP 69571
  • fold Methyltransferase-like (2000088)
    core: 3 layers, a/b/a, mixed beta-sheet of 7 strands, order 3214576, strand 7 is antiparallel to the rest
    Derived from SCOP 53334
  • fold Thiolase-like (2000091)
    consists of two similar subdomains related by pseudo dyad; 5 layers: a/b/a/b/a, two similar mixed beta-sheet of 5 strands each, order: 32451, strand 5 is antiparallel to the rest
    Derived from SCOP 53900
  • fold beta-Grasp (2000097)
    core: beta(2)-alpha-beta(2), 2 layers, a/b; mixed beta-sheet, order: 2143, strands 1 and 4 are parallel to each other
    Derived from SCOP 54235
  • fold Tetrapyrrole methylase C-terminal lobe-like (2000107)
    3 layers, a/b/a; mixed sheet of 5 strands, order 12534, strands 4 & 5 are antiparallel to the rest
    Derived from SCOP 53789
  • fold FUR dimerisation domain-like (2000111)
    dimer of beta(2)-alpha-beta units; mixed beta-sheet, order 213, strand 2 is antiparallel to the rest; forms a single beta-sheet in the dimer with antiparallel H-bonding of strands 3 and 3'
  • fold Nucleotidyltransferase-like (2000113)
    to be split into different fold variants; core: alpha-beta-turn-beta-X-beta-(alpha); mixed beta-sheet, order: 123, strand 1 is antiparallel to the rest
    Derived from SCOP 81302
  • fold E2 binding domain-like (2000122)
    beta-alpha-beta(2)-X-beta(2), 2 layers, a/b; antiparallel beta-sheet 15423
    Circularly permuted variant of the ubiqutin-like topology; the C-terminal strand occupies the position of the N-terminal strand of the ubiquitin-like proteins but runs in the opposite direction