› 1f22

Solution NMR

A PROTON-NMR INVESTIGATION OF THE FULLY REDUCED CYTOCHROME C7 FROM DESULFUROMONAS ACETOXIDANS. COMPARISON BETWEEN THE REDUCED AND THE OXIDIZED FORMS.

Released:
DOI: 10.2210/pdb1f22/pdb
PDB entry 1f22 coloured by chain, ensemble of 35 models, front view.
PDB entry 1f22 coloured by chain, ensemble of 35 models, side view.
PDB entry 1f22 coloured by chain, ensemble of 35 models, top view.
Source organism: Desulfuromonas acetoxidans
Primary publication:
A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms.
Assfalg M, Banci L, Bertini I, Bruschi M, Giudici-Orticoni MT, Turano P
Eur J Biochem 266 634-43 (1999)
PMID: 10561607

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132284 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c3 Chain: A
Molecule details ›
Chain: A
Length: 68 amino acids
Theoretical weight: 7.28 KDa
Source organism: Desulfuromonas acetoxidans
UniProt:
  • Canonical: P00137 (Residues: 1-68; Coverage: 100%)
Gene name: cyd
Structure domains: Cytochrome C3

Ligands and Environments

1 bound ligand:
Ligand HEC 3 x HEC
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing and energy minimization

Quick links

Citations

1 review citation

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Liu et al. (2014)
8 other articles

1 mention without citation

Analysis of conformational variation in macromolecular structural models.
Srivastava et al. (2012)