› 3iea

X-ray diffraction
2.2Å resolution

Structure of reduced M98L mutant of amicyanin

Released:
DOI: 10.2210/pdb3iea/pdb
PDB entry 3iea coloured by chain, front view.
PDB entry 3iea coloured by chain, side view.
PDB entry 3iea coloured by chain, top view.
Source organism: Paracoccus denitrificans
Primary publication:
Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine.
Choi M, Sukumar N, Liu A, Davidson VL
Biochemistry 48 9174-84 (2009)
PMID: 19715303

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
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: 11.49 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

5 bound ligands:
Ligand PO4 1 x PO4
Ligand CU 1 x CU
Ligand ZN 1 x ZN
Ligand CL 1 x CL
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P6322
Unit cell:
a: 99.75Å b: 99.75Å c: 70.74Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.184 0.2
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)
8 other articles

1 mention without citation

Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine.
Choi et al. (2009)