› 3o1y

X-ray diffraction
1.75Å resolution

Electron transfer complexes: Experimental mapping of the redox-dependent cytochrome c electrostatic surface

Released:
DOI: 10.2210/pdb3o1y/pdb
PDB entry 3o1y coloured by chain, front view.
PDB entry 3o1y coloured by chain, side view.
PDB entry 3o1y 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 22 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: P3121
Unit cell:
a: 79.695Å b: 79.695Å c: 89.247Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.186 0.248

Quick links

Citations

1 review citation

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

2 mentions without citation

Distance restraints from crosslinking mass spectrometry: mining a molecular dynamics simulation database to evaluate lysine-lysine distances.
Merkley et al. (2014)
1 more