› 6ss2

X-ray diffraction
2.4Å 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:
hetero nonamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-211524 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Arginase-2, mitochondrial Chain: AAA
Molecule details ›
Chain: AAA
Length: 339 amino acids
Theoretical weight: 37.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P78540 (Residues: 23-354; Coverage: 94%)
Gene name: ARG2
Sequence domains: Arginase family
Fab C0021158 heavy chain (IgG1) Chain: HHH
Molecule details ›
Chain: HHH
Length: 233 amino acids
Theoretical weight: 24.65 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
Fab C0021158 light chain (IgG1) Chain: LLL
Molecule details ›
Chain: LLL
Length: 220 amino acids
Theoretical weight: 23.14 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus

Ligands and Environments

3 bound ligands:
Ligand GOL 20 x GOL
Ligand MN 2 x MN
Ligand SO4 17 x SO4
1 modified residue:
Ligand CSO 1 x CSO

Experiments and Validation Details

Entry percentile scores
R-values:
R R work R free
0.255 0.254 0.284
Expression systems:
  • Escherichia coli BL21(DE3)
  • Cricetulus griseus

Quick links

Citations

1 review citation

Targeting amino acid-metabolizing enzymes for cancer immunotherapy.
Grobben Y. (2024)
2 other articles

4 mentions without citation

Extensive sequence and structural evolution of Arginase 2 inhibitory antibodies enabled by an unbiased approach to affinity maturation.
Chan et al. (2020)
3 more