› 1kdt

X-ray diffraction
1.95Å resolution

CYTIDINE MONOPHOSPHATE KINASE FROM E.COLI IN COMPLEX WITH 2',3'-DIDEOXY-CYTIDINE MONOPHOSPHATE

Released:
DOI: 10.2210/pdb1kdt/pdb
PDB entry 1kdt coloured by chain, front view.
PDB entry 1kdt coloured by chain, side view.
PDB entry 1kdt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme.
Bertrand T, Briozzo P, Assairi L, Ofiteru A, Bucurenci N, Munier-Lehmann H, Golinelli-Pimpaneau B, Bârzu O, Gilles AM
J Mol Biol 315 1099-110 (2002)
PMID: 11827479

Function and Biology Details

Reaction catalysed: 
ATP + (d)CMP = ADP + (d)CDP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141356 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytidylate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 227 amino acids
Theoretical weight: 24.78 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A6I0 (Residues: 1-227; Coverage: 100%)
Gene names: JW0893, b0910, cmk, mssA, ycaF, ycaG
Sequence domains: Cytidylate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand DOC 2 x DOC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 72.648Å b: 75.313Å c: 78.037Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.221 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

19 citation in other articles

Evolution and classification of P-loop kinases and related proteins.
Leipe et al. (2003)
18 more