› 1lm3

X-ray diffraction
2.7Å resolution

A Multi-generation Analysis of Cytochrome b562 Redox Variants: Evolutionary Strategies for Modulating Redox Potential Revealed Using a Library Approach

Released:
DOI: 10.2210/pdb1lm3/pdb
PDB 1lm3 coloured by chain and viewed from the front.
PDB 1lm3 coloured by chain and viewed from the side.
PDB 1lm3 coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
A multigeneration analysis of cytochrome b(562) redox variants: evolutionary strategies for modulating redox potential revealed using a library approach.
Springs SL, Bass SE, Bowman G, Nodelman I, Schutt CE, McLendon GL
Biochemistry 41 4321-8 (2002)
PMID: 11914078

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble cytochrome b562 Chains: B, D
Molecule details ›
Chains: B, D
Length: 106 amino acids
Theoretical weight: 11.74 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABE7 (Residues: 23-128; Coverage: 100%)
Gene name: cybC
Structure domains: Cytochrome c/b562

Ligands and Environments

2 bound ligands:
Ligand MG 3 x MG
Ligand HEM 2 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 42.098Å b: 48.995Å c: 114.419Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.333
Expression system: Escherichia coli

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Citations

5 review citations

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Liu et al. (2014)
4 more