› 1dvh

Solution NMR

STRUCTURE AND DYNAMICS OF FERROCYTOCHROME C553 FROM DESULFOVIBRIO VULGARIS STUDIED BY NMR SPECTROSCOPY AND RESTRAINED MOLECULAR DYNAMICS

Released:
DOI: 10.2210/pdb1dvh/pdb
PDB entry 1dvh coloured by chain, ensemble of 36 models, front view.
PDB entry 1dvh coloured by chain, ensemble of 36 models, side view.
PDB entry 1dvh coloured by chain, ensemble of 36 models, top view.
Source organism: Desulfovibrio vulgaris
Primary publication:
Structure and dynamics of ferrocytochrome c553 from Desulfovibrio vulgaris studied by NMR spectroscopy and restrained molecular dynamics.
Blackledge MJ, Medvedeva S, Poncin M, Guerlesquin F, Bruschi M, Marion D
J Mol Biol 245 661-81 (1995)
PMID: 7844834

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-137322 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c-553 Chain: A
Molecule details ›
Chain: A
Length: 79 amino acids
Theoretical weight: 8.32 KDa
Source organism: Desulfovibrio vulgaris
Expression system: Not provided
UniProt:
  • Canonical: P04032 (Residues: 25-103; Coverage: 100%)
Gene names: DVU_1817, cyf
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Expression system: Not provided

Quick links

Citations

2 review citations

Enzymology and bioenergetics of respiratory nitrite ammonification.
Simon J. (2002)
1 more

2 mentions without citation

Reducing the computational complexity of protein folding via fragment folding and assembly.
Haspel et al. (2003)
1 more