› 2feo

X-ray diffraction
2.8Å resolution

Mutant R188M of The Cytidine Monophosphate Kinase from E. coli complexed with dCMP

Released:
DOI: 10.2210/pdb2feo/pdb
PDB 2feo coloured by chain and viewed from the front.
PDB 2feo coloured by chain and viewed from the side.
PDB 2feo coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase.
Ofiteru A, Bucurenci N, Alexov E, Bertrand T, Briozzo P, Munier-Lehmann H, Gilles AM
FEBS J. 274 3363-73 (2007)
PMID: 17542990

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytidylate kinase Chain: A
Molecule details ›
Chain: A
Length: 227 amino acids
Theoretical weight: 24.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
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 1 x SO4
Ligand DC 1 x DC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P41212
Unit cell:
a: 72.949Å b: 72.949Å c: 76.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.259 0.259 0.339
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Modeling effects of human single nucleotide polymorphisms on protein-protein interactions.
Teng et al. (2009)
10 more

4 mentions without citation

Perspectives on Iron Oxide-Based Materials with Carbon as Anodes for Li- and K-Ion Batteries.
Valvo et al. (2022)
3 more