› 1gr7

X-ray diffraction
1.8Å resolution

Crystal structure of the double mutant Cys3Ser/Ser100Pro from Pseudomonas Aeruginosa at 1.8 A resolution

Released:
DOI: 10.2210/pdb1gr7/pdb
PDB entry 1gr7 coloured by chain, front view.
PDB entry 1gr7 coloured by chain, side view.
PDB entry 1gr7 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Crystal structure of the double azurin mutant Cys3Ser/Ser100Pro from Pseudomonas aeruginosa at 1.8 A resolution: its folding-unfolding energy and unfolding kinetics.
Okvist M, Bonander N, Sandberg A, Karlsson BG, Krengel U, Xue Y, Sjölin L
Biochim Biophys Acta 1596 336-45 (2002)
PMID: 12007613

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132375 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Azurin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 128 amino acids
Theoretical weight: 13.97 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P00282 (Residues: 21-148; Coverage: 100%)
Gene names: PA4922, azu
Sequence domains: Copper binding proteins, plastocyanin/azurin family
Structure domains: Cupredoxins - blue copper proteins

Ligands and Environments

1 bound ligand:
Ligand CU 4 x CU
1 modified residue:
Ligand CSO 4 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 47.79Å b: 100.12Å c: 106.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.208
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Thermostability of proteins: role of metal binding and pH on the stability of the dinuclear CuA site of Thermus thermophilus.
Sujak et al. (2007)

1 mention without citation

Beauty is in the eye of the beholder: proteins can recognize binding sites of homologous proteins in more than one way.
Martin J. (2010)