Structure analysis

Crystal structure of human Arginase-1 complexed with inhibitor 1h

X-ray diffraction
2.001Å resolution
Source organism: Homo sapiens
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: 33375.49 Å2
Buried surface area: 5756.16 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-138411
Assembly 2
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Multimeric state: homo trimer
Accessible surface area: 33116.8 Å2
Buried surface area: 5599.83 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 3
PDBe Complex ID: PDB-CPX-138411

Macromolecules

Chains: A, B
Length: 314 amino acids
Theoretical weight: 33.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P05089 (Residues: 5-318; Coverage: 98%)
Gene name: ARG1
Pfam: Arginase family
InterPro:
CATH: Ureohydrolase domain

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