› 2j4h

X-ray diffraction
2.7Å resolution

Crystal structure of a H121A Escherichia coli dCTP deaminase mutant enzyme

Released:
DOI: 10.2210/pdb2j4h/pdb
PDB entry 2j4h coloured by chain, front view.
PDB entry 2j4h coloured by chain, side view.
PDB entry 2j4h coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme.
Johansson E, Thymark M, Bynck JH, Fanø M, Larsen S, Willemoës M
FEBS J 274 4188-98 (2007)
PMID: 17651436

Function and Biology Details

Reaction catalysed: 
dCTP + H(2)O = dUTP + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dCTP deaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 193 amino acids
Theoretical weight: 21.21 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P28248 (Residues: 1-193; Coverage: 100%)
Gene names: JW2050, b2065, dcd, dus, paxA
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

2 bound ligands:
Ligand YYY 2 x YYY
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P6322
Unit cell:
a: 62.545Å b: 62.545Å c: 342.444Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.225 0.273
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis.
Helt et al. (2008)
8 more