› 1zpg

X-ray diffraction
1.9Å resolution

Arginase I covalently modified with propylamine at Q19C

Released:
DOI: 10.2210/pdb1zpg/pdb
PDB entry 1zpg coloured by chain, front view.
PDB entry 1zpg coloured by chain, side view.
PDB entry 1zpg coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Probing the role of the hyper-reactive histidine residue of arginase.
Colleluori DM, Reczkowski RS, Emig FA, Cama E, Cox JD, Scolnick LR, Compher K, Jude K, Han S, Viola RE, Christianson DW, Ash DE
Arch Biochem Biophys 444 15-26 (2005)
PMID: 16266687

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-139778 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 314 amino acids
Theoretical weight: 33.89 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07824 (Residues: 6-319; Coverage: 97%)
Gene name: Arg1
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

1 bound ligand:
Ligand MN 6 x MN
1 modified residue:
Ligand BPE 3 x BPE

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P32
Unit cell:
a: 88.184Å b: 88.184Å c: 106.652Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 0.22
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Arginase Inhibitors: A Rational Approach Over One Century.
Pudlo et al. (2017)
8 other articles