PDBe 1mq0

X-ray diffraction
2.4Å resolution

Crystal Structure of Human Cytidine Deaminase

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human cytidine deaminase bound to a potent inhibitor.
J. Med. Chem. 48 658-60 (2005)
PMID: 15689149

Function and Biology Details

Reaction catalysed:
2'-deoxycytidine + H(2)O = 2'-deoxyuridine + NH(3)
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytidine deaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 140 amino acids
Theoretical weight: 15.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P32320 (Residues: 11-146; Coverage: 93%)
Gene names: CDA, CDD
Sequence domains: Cytidine and deoxycytidylate deaminase zinc-binding region
Structure domains: Cytidine Deaminase, domain 2

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU ULTRAX 18
Spacegroup: P21212
Unit cell:
a: 52.398Å b: 55.68Å c: 90.689Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.262
Expression system: Escherichia coli BL21