5g1p

X-ray diffraction
3.19Å resolution

Aspartate transcarbamoylase domain of human CAD bound to carbamoyl phosphate

Released:

Function and Biology Details

Reactions catalysed:
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
L-glutamine + H(2)O = L-glutamate + NH(3)
(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate
(1a) ATP + HCO(3)(-) = ADP + carboxyphosphate
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-151063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multifunctional protein CAD Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 314 amino acids
Theoretical weight: 34.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P27708 (Residues: 1915-2225; Coverage: 14%)
Gene name: CAD
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 83.67Å b: 157.67Å c: 83.54Å
α: 90° β: 120.08° γ: 90°
R-values:
R R work R free
0.222 0.221 0.251
Expression system: Escherichia coli BL21(DE3)