› 1ctu

X-ray diffraction
2.3Å resolution

TRANSITION-STATE SELECTIVITY FOR A SINGLE OH GROUP DURING CATALYSIS BY CYTIDINE DEAMINASE

Released:
DOI: 10.2210/pdb1ctu/pdb
PDB entry 1ctu coloured by chain, front view.
PDB entry 1ctu coloured by chain, side view.
PDB entry 1ctu coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Transition-state selectivity for a single hydroxyl group during catalysis by cytidine deaminase.
Xiang S, Short SA, Wolfenden R, Carter CW
Biochemistry 34 4516-23 (1995)
PMID: 7718553

Function and Biology Details

Reaction catalysed: 
2'-deoxycytidine + H(2)O = 2'-deoxyuridine + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytidine deaminase Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 31.57 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0ABF6 (Residues: 1-294; Coverage: 100%)
Gene names: JW2131, b2143, cdd
Sequence domains:
Structure domains: Cytidine Deaminase, domain 2

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand ZEB 1 x ZEB
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 120.3Å b: 120.3Å c: 78.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Not provided

Quick links

Citations

9 review citations

Prediction of binding constants of protein ligands: a fast method for the prioritization of hits obtained from de novo design or 3D database search programs.
Böhm HJ. (1998)
8 more

7 mentions without citation

Low barrier hydrogen bonds in protein structure and function.
Kemp et al. (2021)
6 more