› 1t5k

X-ray diffraction
1.4Å resolution

Crystal structure of amicyanin substituted with cobalt

Released:
DOI: 10.2210/pdb1t5k/pdb
PDB entry 1t5k coloured by chain, front view.
PDB entry 1t5k coloured by chain, side view.
PDB entry 1t5k coloured by chain, top view.
Source organism: Paracoccus denitrificans
Primary publication:
Crystallographic and NMR investigation of cobalt-substituted amicyanin.
Carrell CJ, Wang X, Jones L, Jarrett WL, Davidson VL, Mathews FS
Biochemistry 43 9381-9 (2004)
PMID: 15260481

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 105 amino acids
Theoretical weight: 11.51 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

2 bound ligands:
Ligand CO 4 x CO
Ligand PO4 5 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 57.701Å b: 56.401Å c: 58.706Å
α: 90° β: 99.67° γ: 90°
R-values:
R R work R free
0.184 0.182 0.21
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

1 mention without citation

3D-SURFER: software for high-throughput protein surface comparison and analysis.
La et al. (2009)