› 1lm2

Solution NMR

NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c7

Released:
DOI: 10.2210/pdb1lm2/pdb
PDB 1lm2 coloured by chain and viewed from the front.
PDB 1lm2 coloured by chain and viewed from the side.
PDB 1lm2 coloured by chain and viewed from the top.
Source organism: Desulfuromonas acetoxidans
Primary publication:
The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7).
Assfalg M, Bertini I, Bruschi M, Michel C, Turano P
Proc. Natl. Acad. Sci. U.S.A. 99 9750-4 (2002)
PMID: 12119407

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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
Sequence domains: Cytochrome c7 and related cytochrome c
Structure domains: Cytochrome C3

Ligands and Environments

2 bound ligands:
Ligand CR 1 x CR
Ligand HEC 3 x HEC
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing in torsion angle space

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Citations

1 review citation

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

1 mention without citation

The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7).
Assfalg et al. (2002)