PDBe 1dea

X-ray diffraction
2.1Å resolution

STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION

Released:

Function and Biology Details

Reaction catalysed:
Alpha-D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3). 
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
homo hexamer
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucosamine-6-phosphate deaminase Chains: A, B
Molecule details ›
Chains: A, B
Length: 266 amino acids
Theoretical weight: 29.81 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A759 (Residues: 1-266; Coverage: 100%)
Gene names: JW0664, b0678, glmD, nagB
Sequence domains: Glucosamine-6-phosphate isomerases/6-phosphogluconolactonase
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R32
Unit cell:
a: 125.71Å b: 125.71Å c: 222.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.174 not available
Expression system: Escherichia coli