3tau

X-ray diffraction
2.05Å resolution

Crystal Structure of a Putative Guanylate Monophosphaste Kinase from Listeria monocytogenes EGD-e

Released:
Source organism: Listeria monocytogenes
Entry authors: Brunzelle JS, Wawrzak Z, Onopriyenko O, Kwok J, Anderson WF, Savchenko A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
ATP + GMP = ADP + GDP
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Guanylate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 24.05 KDa
Source organism: Listeria monocytogenes
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8Y672 (Residues: 1-205; Coverage: 100%)
Gene names: gmk, lmo1827
Sequence domains: Guanylate kinase
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 58.733Å b: 65.321Å c: 107.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.22
Expression system: Escherichia coli BL21(DE3)