› 3gmz

X-ray diffraction
1.43Å resolution

Crystal of human arginase in complex with L-ornithine. Resolution 1.43 A.

Released:
DOI: 10.2210/pdb3gmz/pdb
PDB entry 3gmz coloured by chain, front view.
PDB entry 3gmz coloured by chain, side view.
PDB entry 3gmz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design.
Ilies M, Di Costanzo L, Dowling DP, Thorn KJ, Christianson DW
J Med Chem 54 5432-43 (2011)
PMID: 21728378

Function and Biology Details

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

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:
Ligand MN 4 x MN
Ligand ORN 2 x ORN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P3
Unit cell:
a: 90.392Å b: 90.392Å c: 69.422Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.147 0.147 0.185
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
5 more

7 mentions without citation

Binding of α,α-disubstituted amino acids to arginase suggests new avenues for inhibitor design.
Ilies et al. (2011)
6 more