› 5u7f

X-ray diffraction
1.79Å resolution

Co-bound dihydroneopterin triphosphate pyrophosphohydrolase from E. coli

Released:
DOI: 10.2210/pdb5u7f/pdb
PDB entry 5u7f coloured by chain, front view.
PDB entry 5u7f coloured by chain, side view.
PDB entry 5u7f coloured by chain, top view.
Source organism: Escherichia coli O157:H7
Primary publication:
Metal ion coordination in the E. coli Nudix hydrolase dihydroneopterin triphosphate pyrophosphatase: New clues into catalytic mechanism.
Hill SE, Nguyen E, Ukachukwu CU, Freeman DM, Quirk S, Lieberman RL
OpenAccess logo PLoS One 12 e0180241 (2017)
PMID: 28742822

Function and Biology Details

Reaction catalysed: 
7,8-dihydroneopterin 3'-triphosphate + H(2)O = 7,8-dihydroneopterin 3'-phosphate + diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-533196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroneopterin triphosphate diphosphatase Chain: A
Molecule details ›
Chain: A
Length: 150 amino acids
Theoretical weight: 17.33 KDa
Source organism: Escherichia coli O157:H7
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AFC0 (Residues: 1-150; Coverage: 100%)
Gene names: JW1854, b1865, ntpA, nudB
Sequence domains: NUDIX domain
Structure domains: Nucleoside Triphosphate Pyrophosphohydrolase

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand CO 4 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 54.6Å b: 43.09Å c: 57.23Å
α: 90° β: 91.87° γ: 90°
R-values:
R R work R free
0.184 0.177 0.24
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Revitalizing antifolates through understanding mechanisms that govern susceptibility and resistance.
Kordus et al. (2019)
1 other article

1 mention without citation

Metal ion coordination in the E. coli Nudix hydrolase dihydroneopterin triphosphate pyrophosphatase: New clues into catalytic mechanism.
Hill et al. (2017)