Structural Classification of Proteins
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Protein: DNA repair protein Rad51, catalytic domain from Archaeon Methanococcus voltae [TaxId: 2188]

SQ O73948

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a/b) [51349]
    Mainly parallel beta sheets (beta-alpha-beta units)
  3. Fold: P-loop containing nucleoside triphosphate hydrolases [52539]
    3 layers: a/b/a, parallel or mixed beta-sheets of variable sizes
  4. Superfamily: P-loop containing nucleoside triphosphate hydrolases [52540]
    division into families based on beta-sheet topologies
    link to SUPERFAMILY database - Superfamily
  5. Family: RecA protein-like (ATPase-domain) [52670]
    core: mixed beta-sheet of 8 strands, order 32451678; strand 7 is antiparallel to the rest
  6. Protein: DNA repair protein Rad51, catalytic domain [82412]
  7. Species: Archaeon Methanococcus voltae [TaxId: 2188] [110555]
    SQ O73948

PDB Entry Domains:

  1. 2i1q picpicxref
    automatically matched to d1t4ga2
    complexed with anp, ca, mg, na; mutant
    1. region a:65-322 [136985] picpiclink
  2. 1t4g picpicxref
    complexed with anp, mg; mutant
    1. region a:65-322 [106419] picpiclink
  3. 2f1j picpicxref
    automatically matched to d1t4ga2
    complexed with adp, mg; mutant
    1. region a:65-322 [132771] picpiclink
  4. 2b21 picpicxref
    automatically matched to d1t4ga2
    complexed with anp, k, mg; mutant
    1. region a:65-322 [127688] picpiclink
  5. 1xu4 picpicxref
    complexed with anp, k, mg; mutant
    1. region a:65-322 [116046] picpiclink
  6. 2gdj picpic
    automatically matched to d1t4ga2
    complexed with anp, mg
    1. region a:65-322 [135018] picpiclink
  7. 2f1i picpicxref
    automatically matched to d1t4ga2
    complexed with anp, mg; mutant
    1. region a:65-322 [132769] picpiclink
  8. 2f1h picpicxref
    automatically matched to d1t4ga2
    complexed with anp, k, mg; mutant
    1. region a:65-322 [132767] picpiclink
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MRC site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk