› 256b

X-ray diffraction
1.4Å resolution

IMPROVEMENT OF THE 2.5 ANGSTROMS RESOLUTION MODEL OF CYTOCHROME B562 BY REDETERMINING THE PRIMARY STRUCTURE AND USING MOLECULAR GRAPHICS

Released:
DOI: 10.2210/pdb256b/pdb
PDB entry 256b coloured by chain, front view.
PDB entry 256b coloured by chain, side view.
PDB entry 256b coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics.
Lederer F, Glatigny A, Bethge PH, Bellamy HD, Matthew FS
J Mol Biol 148 427-48 (1981)
PMID: 7031264

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142149 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble cytochrome b562 Chains: A, B
Molecule details ›
Chains: A, B
Length: 106 amino acids
Theoretical weight: 11.8 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0ABE7 (Residues: 23-128; Coverage: 100%)
Gene name: cybC
Sequence domains: Cytochrome b562
Structure domains: Cytochrome c/b562

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand HEM 2 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 33.71Å b: 50.48Å c: 32.73Å
α: 102.76° β: 86.55° γ: 106.7°
R-values:
R R work R free
0.164 not available not available
Expression system: Not provided

Quick links

Citations

2 review citations

Structure-function relationships of the alternative oxidase of plant mitochondria: a model of the active site.
Moore et al. (1995)
1 more

35 mentions without citation

Structures and host-adhesion mechanisms of lactococcal siphophages.
Spinelli et al. (2014)
34 more