PDBe 1wvb

X-ray diffraction
2.3Å resolution

Crystal structure of human arginase I: the mutant E256Q

Released:
Source organism: Homo sapiens
Entry authors: Di Costanzo L, Guadalupe S, Mora A, Centeno F, Christianson DW

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
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: ALS BEAMLINE 5.0.2
Spacegroup: P3
Unit cell:
a: 90.272Å b: 90.272Å c: 69.305Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.154 0.154 0.217
Expression system: Escherichia coli