› 1ksu

X-ray diffraction
2Å resolution

Crystal Structure of His505Tyr Mutant Flavocytochrome c3 from Shewanella frigidimarina

Released:
DOI: 10.2210/pdb1ksu/pdb
PDB entry 1ksu coloured by chain, front view.
PDB entry 1ksu coloured by chain, side view.
PDB entry 1ksu coloured by chain, top view.
Source organism: Shewanella frigidimarina
Primary publication:
Role of His505 in the soluble fumarate reductase from Shewanella frigidimarina.
Pankhurst KL, Mowat CG, Miles CS, Leys D, Walkinshaw MD, Reid GA, Chapman SK
Biochemistry 41 8551-6 (2002)
PMID: 12093271

Function and Biology Details

Reaction catalysed: 
Succinate + a quinone = fumarate + a quinol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fumarate reductase (cytochrome) Chains: A, B
Molecule details ›
Chains: A, B
Length: 571 amino acids
Theoretical weight: 60.65 KDa
Source organism: Shewanella frigidimarina
Expression system: Shewanella frigidimarina
UniProt:
  • Canonical: P0C278 (Residues: 1-571; Coverage: 100%)
Gene names: fcc3, fccA
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand HEM 8 x HEM
2 bound ligands:
Ligand NA 2 x NA
Ligand FUM 2 x FUM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21
Unit cell:
a: 76.989Å b: 87.274Å c: 89.366Å
α: 90° β: 104.43° γ: 90°
R-values:
R R work R free
0.167 0.167 0.239
Expression system: Shewanella frigidimarina

Quick links

Citations

4 review citations

Function and structure of complex II of the respiratory chain.
Cecchini G. (2003)
3 more

1 mention without citation

Imidazole and nitroimidazole derivatives as NADH-fumarate reductase inhibitors: Density functional theory studies, homology modeling, and molecular docking.
Campos-Fernández et al. (2022)