› 2anb

X-ray diffraction
2.9Å resolution

Crystal Structure Of Oligomeric E.coli Guanylate Kinase In Complex With GMP

Released:
DOI: 10.2210/pdb2anb/pdb
PDB entry 2anb coloured by chain, front view.
PDB entry 2anb coloured by chain, side view.
PDB entry 2anb coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Calorimetric and crystallographic analysis of the oligomeric structure of Escherichia coli GMP kinase.
Hible G, Renault L, Schaeffer F, Christova P, Zoe Radulescu A, Evrin C, Gilles AM, Cherfils J
J Mol Biol 352 1044-59 (2005)
PMID: 16140325

Function and Biology Details

Reaction catalysed: 
ATP + GMP = ADP + GDP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo hexamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158040 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanylate kinase Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 23.63 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P60546 (Residues: 1-207; Coverage: 100%)
Gene names: JW3623, b3648, gmk, spoR
Sequence domains: Guanylate kinase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand 5GP 1 x 5GP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: R32
Unit cell:
a: 106.728Å b: 106.728Å c: 155.276Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.242
Expression system: Escherichia coli

Quick links

Citations

15 citation in other articles

Cross-talk between phosphorylation and lysine acetylation in a genome-reduced bacterium.
van Noort et al. (2012)
14 more

4 mentions without citation

Molecular mechanism and evolution of guanylate kinase regulation by (p)ppGpp.
Liu et al. (2015)
3 more