PDBe 4fck

X-ray diffraction
1.9Å resolution

Crystal Structure of the Co2+2-Human Arginase I-AGPA Complex

Released:
Source organism: Homo sapiens
Primary publication:
Binding of the unreactive substrate analog L-2-amino-3-guanidinopropionic acid (dinor-L-arginine) to human arginase I.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 889-93 (2012)
PMID: 22869115

Function and Biology Details

Reaction catalysed:
L-arginine + H(2)O = L-ornithine + urea
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 34.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05089 (Residues: 1-322; Coverage: 100%)
Gene name: ARG1
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P3
Unit cell:
a: 90.451Å b: 90.451Å c: 69.362Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.273 0.273 0.307
Expression system: Escherichia coli BL21(DE3)