6hg3

X-ray diffraction
1.97Å resolution

Hybrid dihydroorotase domain of human CAD with E. coli flexible loop, bound to dihydroorotate

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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-151062 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multifunctional protein CAD Chain: A
Molecule details ›
Chain: A
Length: 371 amino acids
Theoretical weight: 40.33 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P27708 (Residues: 1456-1559, 1561-1822; Coverage: 16%)
Gene name: CAD
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2221
Unit cell:
a: 81.909Å b: 159.472Å c: 61.878Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.19
Expression system: Homo sapiens