› 1qq3

Solution NMR

THE SOLUTION STRUCTURE OF THE HEME BINDING VARIANT ARG98CYS OF OXIDIZED ESCHERICHIA COLI CYTOCHROME B562

Released:
DOI: 10.2210/pdb1qq3/pdb
PDB entry 1qq3 coloured by chain, front view.
PDB entry 1qq3 coloured by chain, side view.
PDB entry 1qq3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural consequences of b- to c-type heme conversion in oxidized Escherichia coli cytochrome b562.
Arnesano F, Banci L, Bertini I, Ciofi-Baffoni S, Woodyear TL, Johnson CM, Barker PD
Biochemistry 39 1499-514 (2000)
PMID: 10684632

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 Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ABE7 (Residues: 23-128; Coverage: 100%)
Gene name: cybC
Sequence domains: Cytochrome b562
Structure domains: Cytochrome c/b562

Ligands and Environments

1 bound ligand:
Ligand HEB 1 x HEB
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: TORSION ANGLE DYNAMICS FOLLOWED BY ENERGY MINIMIZATION
Expression system: Escherichia coli

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Citations

6 review citations

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

1 mention without citation

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Yadav et al. (2022)