Hyperfamilies

  • hyperfamily DNA/RNA-binding 3-helical bundle (1100001)
    core: 3-helices, bundle, closed or partly opened, right-handed twist, up-and down
    Derived from SCOP 46688
  • hyperfamily Rossmann-like nucleotide-binding lobe (1100002)
    3 layer core: alpha/beta/alpha, parallel beta-sheet of 6 strands, order 321456; common region begins with strand 1 and ends with strand 6; the core is packed against the helix that, depending on a particular superfamily member, either precedes strands 1 (rare), or follows strand 6 (common)
    Derived from SCOP 51734
  • hyperfamily Multiheme cytochromes (1100003)
    variable number of helices and little beta structure, not a true fold
    Derived from SCOP 48694
  • hyperfamily FAD/NAD(P)-binding domain (1100004)
    core: 3 layers, b/b/a, central parallel beta-sheet of 5 strands, order 32145, top antiparallel beta-sheet of 3 strands, meander
    Derived from SCOP 51904
  • hyperfamily Ribokinase-like (1100005)
    core: 3 layers: a/b/a, mixed beta-sheet of 8 strands, order 21345678, strand 7 is antiparallel to the rest
    members of this hyperfamily have similar functions but different ATP-binding sites
    Derived from SCOP 53612
  • hyperfamily ATP-grasp (1100006)
    Consists of two subdomains with different alpha+beta folds shares functional and structural similarities with the PIPK and protein kinase superfamilies
    Derived from SCOP 56058
  • hyperfamily Ntn hydrolase-like (1100007)
    4 layers: alpha/beta/beta/alpha, has an unusual sheet-to-sheet packing
    Derived from SCOP 56234
  • hyperfamily CC domain-like (1100008)
    3-helices, bundle, up-and-down, right-handed twist
  • hyperfamily Ubiquitin-like (1100009)
    beta(2)-alpha-beta(2)-X-beta; 2 layers, a/b/; mixed beta-sheet, order: 21534, strands 1 and 5 are parallel to each other
  • hyperfamily P-loop containing nucleoside triphosphate hydrolases (1100010)
    Hyperfamily region have spans from the strand preceding the P-loop motif to the strand that flanks the P-loop strand at the 'nucleoside' side; the numbers of strands and topology of beta-sheet on the 'triphosphate' side may vary greatly
    Derived from SCOP 52539