› 4c6f

X-ray diffraction
1.26Å resolution

Crystal structure of the dihydroorotase domain of human CAD bound to substrate at pH 6.5

Released:
DOI: 10.2210/pdb4c6f/pdb
PDB 4c6f coloured by chain and viewed from the front.
PDB 4c6f coloured by chain and viewed from the side.
PDB 4c6f coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Structure, Functional Characterization, and Evolution of the Dihydroorotase Domain of Human CAD.
Grande-García A, Lallous N, Díaz-Tejada C, Ramón-Maiques S
Structure (2013)
PMID: 24332717

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CAD protein Chain: A
Molecule details ›
Chain: A
Length: 393 amino acids
Theoretical weight: 42.92 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P27708 (Residues: 1456-1846; Coverage: 18%)
Gene name: CAD
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

4 bound ligands:
Ligand DOR 1 x DOR
Ligand NCD 1 x NCD
Ligand ZN 4 x ZN
Ligand FMT 4 x FMT
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 82.17Å b: 158.87Å c: 61.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.123 0.123 0.136
Expression system: Homo sapiens

Quick links

Citations

1 review citation

From Genome to Structure and Back Again: A Family Portrait of the Transcarbamylases.
Shi et al. (2015)
18 other articles