4a7x

X-ray diffraction
2.49Å resolution

Crystal structure of uridylate kinase from Helicobacter pylori

Released:
Source organism: Helicobacter pylori 26695
Entry authors: Chu CH, Liu MH, Chen PC, Sun YJ

Function and Biology Details

Reaction catalysed:
ATP + UMP = ADP + UDP
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uridylate kinase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 240 amino acids
Theoretical weight: 26.21 KDa
Source organism: Helicobacter pylori 26695
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P56106 (Residues: 1-240; Coverage: 100%)
Gene names: HP_0777, pyrH
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: C2
Unit cell:
a: 147.136Å b: 127.627Å c: 93.181Å
α: 90° β: 91.46° γ: 90°
R-values:
R R work R free
0.216 0.213 0.276
Expression system: Escherichia coli K-12