› 351c

X-ray diffraction
1.6Å resolution

STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO REDOX FORMS

Released:
DOI: 10.2210/pdb351c/pdb
PDB entry 351c coloured by chain, front view.
PDB entry 351c coloured by chain, side view.
PDB entry 351c coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 A resolution and comparison of the two redox forms.
Matsuura Y, Takano T, Dickerson RE
J Mol Biol 156 389-409 (1982)
PMID: 6283101

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-132247 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c-551 Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 8.7 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Not provided
UniProt:
  • Canonical: P00099 (Residues: 23-104; Coverage: 100%)
Gene names: PA0518, nirM
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 29.5Å b: 49.27Å c: 49.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 not available
Expression system: Not provided

Quick links

Citations

7 review citations

Cell biology and molecular basis of denitrification.
Zumft WG. (1997)
6 more

23 mentions without citation

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