Structural Classification of Proteins
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Protein: Fumarate reductase iron-sulfur protein, N-terminal domain from Escherichia coli [TaxId: 562]

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: beta-Grasp (ubiquitin-like) [54235]
    core: beta(2)-alpha-beta(2); mixed beta-sheet 2143
  4. Superfamily: 2Fe-2S ferredoxin-like [54292]
    link to SUPERFAMILY database - Superfamily
  5. Family: 2Fe-2S ferredoxin domains from multidomain proteins [54312]
  6. Protein: Fumarate reductase iron-sulfur protein, N-terminal domain [54325]
  7. Species: Escherichia coli [TaxId: 562] [54326]

PDB Entry Domains:

  1. 1kf6 picpicxrefxrefxrefxrefxrefxref
    complexed with 1pe, act, ce1, f3s, fad, fes, fs4, hqo, k, oaa
    1. region b:1-105 [72398] picpiclink
    2. region n:1-105 [72405] picpiclink
  2. 1l0v picpicxrefxrefxrefxrefxrefxref
    complexed with ce1, f3s, fad, fes, fs4, mq7, oaa
    1. region b:1-105 [73416] picpiclink
    2. region n:1-105 [73423] picpiclink
  3. 1kfy picpicxrefxrefxrefxrefxrefxref
    complexed with brs, ce1, f3s, fad, fes, fs4, oaa
    1. region b:1-105 [72431] picpiclink
    2. region n:1-105 [72438] picpiclink
  4. 3cir picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6b2
    complexed with f3s, fad, fes, sf4; mutant
    1. region b:1-105 [156683] picpiclink
  5. 3cir picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6b2
    complexed with f3s, fad, fes, sf4; mutant
    1. region n:1-105 [156690] picpiclink
  6. 2b76 picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6b2
    complexed with f3s, fad, fes, flc, mq7, sf4; mutant
    1. region b:1-105 [128013] picpiclink
  7. 2b76 picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6b2
    complexed with f3s, fad, fes, flc, mq7, sf4; mutant
    1. region n:1-105 [128020] 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