› 2rac

X-ray diffraction
1.3Å resolution

AMICYANIN REDUCED, PH 7.7, 1.3 ANGSTROMS

Released:
DOI: 10.2210/pdb2rac/pdb
PDB entry 2rac coloured by chain, front view.
PDB entry 2rac coloured by chain, side view.
PDB entry 2rac coloured by chain, top view.
Source organism: Paracoccus denitrificans
Primary publication:
Molecular basis for interprotein complex-dependent effects on the redox properties of amicyanin.
Zhu Z, Cunane LM, Chen Z, Durley RC, Mathews FS, Davidson VL
Biochemistry 37 17128-36 (1998)
PMID: 9860825

Function and Biology Details

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

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: 11.51 KDa
Source organism: Paracoccus denitrificans
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 1 x CU1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 28.75Å b: 56.2Å c: 27.42Å
α: 90° β: 96.12° γ: 90°
R-values:
R R work R free
0.182 0.182 0.21

Quick links

Citations

6 review citations

Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes.
Choi et al. (2011)
5 more

8 mentions without citation

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