› 1nt4

X-ray diffraction
2.4Å resolution

Crystal structure of Escherichia coli periplasmic glucose-1-phosphatase H18A mutant complexed with glucose-1-phosphate

Released:
DOI: 10.2210/pdb1nt4/pdb
PDB entry 1nt4 coloured by chain, front view.
PDB entry 1nt4 coloured by chain, side view.
PDB entry 1nt4 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Functional insights revealed by the crystal structures of Escherichia coli glucose-1-phosphatase.
Lee DC, Cottrill MA, Forsberg CW, Jia Z
J Biol Chem 278 31412-8 (2003)
PMID: 12782623

Function and Biology Details

Reaction catalysed: 
Alpha-D-glucose 1-phosphate + H(2)O = D-glucose + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-1-phosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 391 amino acids
Theoretical weight: 43.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P19926 (Residues: 23-413; Coverage: 100%)
Gene names: JW0987, agp, b1002
Sequence domains: Histidine phosphatase superfamily (branch 2)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

1 bound ligand:
Ligand XGP 2 x XGP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: R3
Unit cell:
a: 156.263Å b: 156.263Å c: 84.575Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.218 0.284
Expression system: Escherichia coli

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Citations

1 review citation

Research status of Bacillus phytase.
Zhao et al. (2021)
17 other articles

5 mentions without citation

Contribution of structural genomics to understanding the biology of Escherichia coli.
Matte et al. (2003)
4 more