› 2we4

X-ray diffraction
2.02Å resolution

Carbamate kinase from Enterococcus faecalis bound to a sulfate ion and two water molecules, which mimic the substrate carbamyl phosphate

Released:
DOI: 10.2210/pdb2we4/pdb
PDB entry 2we4 coloured by chain, front view.
PDB entry 2we4 coloured by chain, side view.
PDB entry 2we4 coloured by chain, top view.
Source organism: Enterococcus faecalis
Primary publication:
Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria.
Ramón-Maiques S, Marina A, Guinot A, Gil-Ortiz F, Uriarte M, Fita I, Rubio V
J Mol Biol 397 1261-75 (2010)
PMID: 20188742

Function and Biology Details

Reaction catalysed: 
(1a) ATP + carbamate = ADP + carbamoyl phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141077 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carbamate kinase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 310 amino acids
Theoretical weight: 32.96 KDa
Source organism: Enterococcus faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A2X7 (Residues: 1-310; Coverage: 100%)
Gene names: EF_0106, arcC, arcC-1, arcC1
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

1 bound ligand:
Ligand SO4 15 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 80.888Å b: 172.6Å c: 98.627Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.234
Expression system: Escherichia coli

Quick links

Citations

14 citation in other articles

Visualizing autophosphorylation in histidine kinases.
Casino et al. (2014)
13 more

2 mentions without citation

Sources and Fates of Carbamyl Phosphate: A Labile Energy-Rich Molecule with Multiple Facets.
Shi et al. (2018)
1 more