› 1d4c

X-ray diffraction
2.9Å resolution

CRYSTAL STRUCTURE OF THE UNCOMPLEXED FORM OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1

Released:
DOI: 10.2210/pdb1d4c/pdb
PDB entry 1d4c coloured by chain, front view.
PDB entry 1d4c coloured by chain, side view.
PDB entry 1d4c coloured by chain, top view.
Source organism: Shewanella oneidensis
Primary publication:
Structure and mechanism of the flavocytochrome c fumarate reductase of Shewanella putrefaciens MR-1.
Leys D, Tsapin AS, Nealson KH, Meyer TE, Cusanovich MA, Van Beeumen JJ
Nat Struct Biol 6 1113-7 (1999)
PMID: 10581551

Function and Biology Details

Reaction catalysed: 
Succinate + a quinone = fumarate + a quinol
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160678 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fumarate reductase (cytochrome) Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 572 amino acids
Theoretical weight: 59.97 KDa
Source organism: Shewanella oneidensis
UniProt:
  • Canonical: P83223 (Residues: 25-596; Coverage: 100%)
Gene names: SO_0970, fccA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand HEC 16 x HEC

Cofactor: Ligand FAD 4 x FAD
1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE D41A
Spacegroup: P21212
Unit cell:
a: 109.69Å b: 216.36Å c: 112.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.3

Quick links

Citations

18 review citations

Sequence-structure analysis of FAD-containing proteins.
Dym et al. (2001)
17 more

6 mentions without citation

Networks of high mutual information define the structural proximity of catalytic sites: implications for catalytic residue identification.
Marino Buslje et al. (2010)
5 more