› 4hfq

X-ray diffraction
1.39Å resolution

Crystal structure of UDP-X diphosphatase

Released:
DOI: 10.2210/pdb4hfq/pdb
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PDB entry 4hfq coloured by chain, front view.
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Source organism: Streptococcus pneumoniae TIGR4
Primary publication:
A UDP-X diphosphatase from Streptococcus pneumoniae hydrolyzes precursors of peptidoglycan biosynthesis.
Duong-Ly KC, Woo HN, Dunn CA, Xu W, Babič A, Bessman MJ, Amzel LM, Gabelli SB
OpenAccess logo PLoS One 8 e64241 (2013)
PMID: 23691178

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nudix hydrolase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 203 amino acids
Theoretical weight: 23.49 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H2URA0 (Residues: 1-203; Coverage: 100%)
Gene name: SP_1669
Sequence domains:
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

6 bound ligands:
Ligand EDO 11 x EDO
Ligand TRS 3 x TRS
Ligand SO4 5 x SO4
Ligand PEG 4 x PEG
Ligand GOL 6 x GOL
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P31
Unit cell:
a: 77.992Å b: 77.992Å c: 64.704Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.172 0.196
Expression system: Escherichia coli

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Citations

2 citation in other articles

Contribution of the Pseudomonas fluorescens MFE01 Type VI Secretion System to Biofilm Formation.
Gallique et al. (2017)
1 more

1 mention without citation

A UDP-X diphosphatase from Streptococcus pneumoniae hydrolyzes precursors of peptidoglycan biosynthesis.
Duong-Ly et al. (2013)

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