Structure analysis

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

X-ray diffraction
2.74Å resolution
Source organism: Rattus norvegicus
Assembly composition:
homo trimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo trimer
Accessible surface area: 34208.86 Å2
Buried surface area: 5830.55 Å2
Dissociation area: 2,723.83 Å2
Dissociation energy (ΔGdiss): 11.15 kcal/mol
Dissociation entropy (TΔSdiss): 27.57 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-139779

Macromolecules

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
Pfam: Arginase family
InterPro:
CATH: Ureohydrolase domain
SCOP: Arginase-like amidino hydrolases

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