› 7klk

X-ray diffraction
1.8Å resolution

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-138411 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 322 amino acids
Theoretical weight: 34.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P05089 (Residues: 1-322; Coverage: 100%)
Gene name: ARG1
Sequence domains: Arginase family

Ligands and Environments

3 bound ligands:
Ligand MN 12 x MN
Ligand XFP 6 x XFP
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 53.157Å b: 281.463Å c: 67.078Å
α: 90° β: 90.06° γ: 90°
R-values:
R R work R free
0.206 0.204 0.236
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The expanding role for small molecules in immuno-oncology.
Offringa et al. (2022)
1 more

1 mention without citation

Structure-Based Discovery of Proline-Derived Arginase Inhibitors with Improved Oral Bioavailability for Immuno-Oncology.
Lu et al. (2021)