› 3o20

X-ray diffraction
1.9Å resolution

Electron transfer complexes:experimental mapping of the Redox-dependent Cytochrome C electrostatic surface

Released:
DOI: 10.2210/pdb3o20/pdb
Model geometry
Fit model/data
PDB entry 3o20 coloured by chain, front view.
PDB entry 3o20 coloured by chain, side view.
PDB entry 3o20 coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Nitrate as a probe of cytochrome c surface: crystallographic identification of crucial "hot spots" for protein-protein recognition.
De March M, Demitri N, De Zorzi R, Casini A, Gabbiani C, Guerri A, Messori L, Geremia S
J Inorg Biochem 135 58-67 (2014)
PMID: 24662464

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132211 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 105 amino acids
Theoretical weight: 11.75 KDa
Source organism: Equus caballus
UniProt:
  • Canonical: P00004 (Residues: 2-105; Coverage: 99%)
Gene names: CYC, CYCS
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain

Ligands and Environments

2 bound ligands:
Ligand HEC 3 x HEC
Ligand NO3 18 x NO3
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: C2
Unit cell:
a: 90.092Å b: 52.029Å c: 77.749Å
α: 90° β: 123.07° γ: 90°
R-values:
R R work R free
0.197 0.193 0.276

Quick links

Citations

1 review citation

Atomic Details of Carbon-Based Nanomolecules Interacting with Proteins.
Di Costanzo et al. (2020)
5 other articles

1 mention without citation

Complex structure of cytochrome c-cytochrome c oxidase reveals a novel protein-protein interaction mode.
Shimada et al. (2017)