› 1xs1

X-ray diffraction
1.8Å resolution

dCTP deaminase from Escherichia coli in complex with dUTP

Released:
DOI: 10.2210/pdb1xs1/pdb
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Source organism: Escherichia coli
Primary publication:
Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes.
Johansson E, Fanø M, Bynck JH, Neuhard J, Larsen S, Sigurskjold BW, Christensen U, Willemoës M
J Biol Chem 280 3051-9 (2005)
PMID: 15539408

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-151183 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dCTP deaminase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 193 amino acids
Theoretical weight: 21.28 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P28248 (Residues: 1-193; Coverage: 100%)
Gene names: JW2050, b2065, dcd, dus, paxA
Sequence domains: dCTP deaminase-like
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

2 bound ligands:
Ligand MG 6 x MG
Ligand DUT 6 x DUT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 63.035Å b: 97.461Å c: 95.475Å
α: 90° β: 109.23° γ: 90°
R-values:
R R work R free
0.164 0.164 0.195
Expression system: Escherichia coli BL21(DE3)

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Citations

16 citation in other articles

House cleaning, a part of good housekeeping.
Galperin et al. (2006)
15 more

3 mentions without citation

Nucleotide pyrophosphatase employs a P-loop-like motif to enhance catalytic power and NDP/NTP discrimination.
Pécsi et al. (2011)
2 more

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