Structure analysis

Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline

X-ray diffraction
2.4Å resolution
Source organism: Homo sapiens
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo tetramer
Accessible surface area: 54700 Å2
Buried surface area: 28500 Å2
Dissociation area: 1,400 Å2
Dissociation energy (ΔGdiss): -22 kcal/mol
Dissociation entropy (TΔSdiss): 16 kcal/mol
Interface energy (ΔGint): -129 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 413 amino acids
Theoretical weight: 46.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00966 (Residues: 1-412; Coverage: 100%)
Gene names: ASS, ASS1
Pfam: Arginosuccinate synthase
InterPro:
CATH:

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