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: Globin-like [46457]
    core: 6 helices; folded leaf, partly opened
  4. Superfamily: alpha-helical ferredoxin [46548]
    contains two Fe4-S4 clusters
    link to SUPERFAMILY database - Superfamily
  5. Family: Fumarate reductase/Succinate dehydogenase iron-sulfur protein, C-terminal domain [46549]
  6. Protein: Fumarate reductase [46550]
  7. Species: Escherichia coli [TaxId: 562] [46551]

PDB Entry Domains:

  1. 1kf6 picpicxrefxrefxrefxrefxrefxref
    complexed with 1pe, act, ce1, f3s, fad, fes, fs4, hqo, k, oaa
    1. region b:106-243 [72397] picpiclink
    2. region n:106-243 [72404] picpiclink
  2. 1l0v picpicxrefxrefxrefxrefxrefxref
    complexed with ce1, f3s, fad, fes, fs4, mq7, oaa
    1. region b:106-243 [73415] picpiclink
    2. region n:106-243 [73422] picpiclink
  3. 1kfy picpicxrefxrefxrefxrefxrefxref
    complexed with brs, ce1, f3s, fad, fes, fs4, oaa
    1. region b:106-243 [72430] picpiclink
    2. region n:106-243 [72437] picpiclink
  4. 3cir picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6b1
    complexed with f3s, fad, fes, sf4; mutant
    1. region b:106-243 [156682] picpiclink
  5. 3cir picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6b1
    complexed with f3s, fad, fes, sf4; mutant
    1. region n:106-243 [156689] picpiclink
  6. 2b76 picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6b1
    complexed with f3s, fad, fes, flc, mq7, sf4; mutant
    1. region b:106-243 [128012] picpiclink
  7. 2b76 picpicxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxrefxref
    automatically matched to d1kf6b1
    complexed with f3s, fad, fes, flc, mq7, sf4; mutant
    1. region n:106-243 [128019] 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