› 2gba

X-ray diffraction
0.92Å resolution

Reduced Cu(I) form at pH 4 of P52G mutant of amicyanin

Released:
DOI: 10.2210/pdb2gba/pdb
PDB entry 2gba coloured by chain, front view.
PDB entry 2gba coloured by chain, side view.
PDB entry 2gba coloured by chain, top view.
Source organism: Paracoccus denitrificans
Primary publication:
Site-directed mutagenesis of proline 52 to glycine in amicyanin converts a true electron transfer reaction into one that is conformationally gated.
Ma JK, Carrell CJ, Mathews FS, Davidson VL
Biochemistry 45 8284-93 (2006)
PMID: 16819827

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149611 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amicyanin Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.47 KDa
Source organism: Paracoccus denitrificans
Expression system: Escherichia coli
UniProt:
  • Canonical: P22364 (Residues: 27-131; Coverage: 100%)
Gene names: ami, mauC
Sequence domains: Copper binding proteins, plastocyanin/azurin family
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

1 bound ligand:
Ligand CU1 2 x CU1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 28.45Å b: 56.132Å c: 27.003Å
α: 90° β: 96.98° γ: 90°
R-values:
R R work R free
0.111 not available 0.148
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Mechanisms for control of biological electron transfer reactions.
Williamson et al. (2014)
5 other articles

1 mention without citation

The oxygen-oxygen distance of water in crystallographic data sets.
Palese LL. (2020)