› 1cno

X-ray diffraction
2.2Å resolution

STRUCTURE OF PSEUDOMONAS NAUTICA CYTOCHROME C552, BY MAD METHOD

Released:
DOI: 10.2210/pdb1cno/pdb
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PDB entry 1cno coloured by chain, front view.
PDB entry 1cno coloured by chain, side view.
PDB entry 1cno coloured by chain, top view.
Source organism: Marinobacter nauticus
Primary publication:
MAD structure of Pseudomonas nautica dimeric cytochrome c552 mimicks the c4 Dihemic cytochrome domain association.
Brown K, Nurizzo D, Besson S, Shepard W, Moura J, Moura I, Tegoni M, Cambillau C
J Mol Biol 289 1017-28 (1999)
PMID: 10369779

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160652 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c-552 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 87 amino acids
Theoretical weight: 8.71 KDa
Source organism: Marinobacter nauticus
UniProt:
  • Canonical: P82903 (Residues: 1-84; Coverage: 96%)
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain

Ligands and Environments

2 bound ligands:
Ligand HEC 8 x HEC
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID09
Spacegroup: P3112
Unit cell:
a: 121.8Å b: 121.8Å c: 136.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.178 0.208

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Citations

1 review citation

Diversity of protein-protein interactions.
Nooren et al. (2003)
15 other articles

4 mentions without citation

Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface.
Siglioccolo et al. (2011)
3 more

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