Structural Classification of Proteins
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Protein: Fumarate reductase from Escherichia coli [TaxId: 562]

Lineage:

  1. Root: scop
  2. Class: All alpha proteins [46456]
  3. Fold: Spectrin repeat-like [46965]
    3 helices; bundle, closed, left-handed twist; up-and-down
  4. Superfamily: Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain [46977]
    link to SUPERFAMILY database - Superfamily
  5. Family: Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain [46978]
  6. Protein: Fumarate reductase [46981]
  7. Species: Escherichia coli [TaxId: 562] [46982]

PDB Entry Domains:

  1. 1kf6 picpicxrefxrefxrefxrefxrefxref
    complexed with 1pe, act, ce1, f3s, fad, fes, fs4, hqo, k, oaa
    1. region a:443-576 [72394] picpiclink
    2. region m:443-576 [72401] picpiclink
  2. 1l0v picpicxrefxrefxrefxrefxrefxref
    complexed with ce1, f3s, fad, fes, fs4, mq7, oaa
    1. region a:443-576 [73412] picpiclink
    2. region m:443-576 [73419] picpiclink
  3. 1kfy picpicxrefxrefxrefxrefxrefxref
    complexed with brs, ce1, f3s, fad, fes, fs4, oaa
    1. region a:443-576 [72427] picpiclink
    2. region m:443-576 [72434] picpiclink
  4. 3cir picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6a1
    complexed with f3s, fad, fes, sf4; mutant
    1. region a:443-576 [156679] picpiclink
  5. 3cir picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6a1
    complexed with f3s, fad, fes, sf4; mutant
    1. region m:443-571 [156686] picpiclink
  6. 2b76 picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6a1
    complexed with f3s, fad, fes, flc, mq7, sf4; mutant
    1. region a:443-576 [128009] picpiclink
  7. 2b76 picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6a1
    complexed with f3s, fad, fes, flc, mq7, sf4; mutant
    1. region m:443-571 [128016] 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