X-ray diffraction
2.4Å resolution

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

Source organism: Homo sapiens
Primary publication:
Structure of human argininosuccinate synthetase.
Acta Crystallogr. D Biol. Crystallogr. 64 279-86 (2008)
PMID: 18323623

Function and Biology Details

Reaction catalysed:
ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Argininosuccinate synthase Chain: A
Molecule details ›
Chain: A
Length: 413 amino acids
Theoretical weight: 46.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P00966 (Residues: 1-412; Coverage: 100%)
Gene names: ASS, ASS1
Sequence domains: Arginosuccinate synthase
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: F222
Unit cell:
a: 95.94Å b: 117.47Å c: 155.15Å
α: 90° β: 90° γ: 90°
R R work R free
0.198 0.194 0.265
Expression system: Escherichia coli BL21(DE3)