› 1h29

X-ray diffraction
2.51Å resolution

Sulfate respiration in Desulfovibrio vulgaris Hildenborough: Structure of the 16-heme Cytochrome c HmcA at 2.5 A resolution and a view of its role in transmembrane electron transfer

Released:
DOI: 10.2210/pdb1h29/pdb
PDB entry 1h29 coloured by chain, front view.
PDB entry 1h29 coloured by chain, side view.
PDB entry 1h29 coloured by chain, top view.
Source organism: Desulfovibrio vulgaris str. Hildenborough
Primary publication:
Sulfate respiration in Desulfovibrio vulgaris Hildenborough. Structure of the 16-heme cytochrome c HmcA AT 2.5-A resolution and a view of its role in transmembrane electron transfer.
Matias PM, Coelho AV, Valente FM, Plácido D, LeGall J, Xavier AV, Pereira IA, Carrondo MA
J Biol Chem 277 47907-16 (2002)
PMID: 12356749

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150155 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High-molecular-weight cytochrome c Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 514 amino acids
Theoretical weight: 55.77 KDa
Source organism: Desulfovibrio vulgaris str. Hildenborough
UniProt:
  • Canonical: P24092 (Residues: 32-545; Coverage: 100%)
Gene names: DVU_0536, hmc, hmcA
Sequence domains: Class III cytochrome C family
Structure domains: Cytochrome C3

Ligands and Environments

1 bound ligand:
Ligand HEC 64 x HEC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P62
Unit cell:
a: 220.39Å b: 220.39Å c: 102.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.192 0.258

Quick links

Citations

4 review citations

The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism.
Venceslau et al. (2014)
3 more

1 mention without citation

The chemistry and biochemistry of heme c: functional bases for covalent attachment.
Bowman et al. (2008)