› 5rla

X-ray diffraction
2.74Å resolution

ALTERING THE BINUCLEAR MANGANESE CLUSTER OF ARGINASE DIMINISHES THERMOSTABILITY AND CATALYTIC FUNCTION

Released:
DOI: 10.2210/pdb5rla/pdb
PDB entry 5rla coloured by chain, front view.
PDB entry 5rla coloured by chain, side view.
PDB entry 5rla coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Altering the binuclear manganese cluster of arginase diminishes thermostability and catalytic function.
Scolnick LR, Kanyo ZF, Cavalli RC, Ash DE, Christianson DW
Biochemistry 36 10558-65 (1997)
PMID: 9265637

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

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139779 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginase-1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 323 amino acids
Theoretical weight: 35 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07824 (Residues: 1-323; Coverage: 100%)
Gene name: Arg1
Sequence domains: Arginase family
Structure domains: Ureohydrolase domain

Ligands and Environments

1 bound ligand:
Ligand MN 3 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P32
Unit cell:
a: 88.9Å b: 88.9Å c: 105.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.175 0.27
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes.
Christianson et al. (1999)
1 more