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Solution NMR

THE Y64A MUTANT OF CYTOCHROME C553 FROM DESULFOVIBRIO VULGARIS HILDENBOROUGH, NMR, 39 STRUCTURES

Released:
DOI: 10.2210/pdb2dvh/pdb
PDB entry 2dvh coloured by chain, ensemble of 39 models, front view.
PDB entry 2dvh coloured by chain, ensemble of 39 models, side view.
PDB entry 2dvh coloured by chain, ensemble of 39 models, top view.
Source organism: Desulfovibrio vulgaris str. Hildenborough
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: 8.23 KDa
Source organism: Desulfovibrio vulgaris str. Hildenborough
Expression system: Desulfovibrio desulfuricans
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
Refinement method: SIMULATED ANNEALING AND RESTRAINED MOLECULAR DYNAMICS ENERGY REFINEMENT
Expression system: Desulfovibrio desulfuricans

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Citations

2 review citations

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