› 1cd5

X-ray diffraction
2.3Å resolution

GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER

Released:
DOI: 10.2210/pdb1cd5/pdb
PDB entry 1cd5 coloured by chain, front view.
PDB entry 1cd5 coloured by chain, side view.
PDB entry 1cd5 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution.
Horjales E, Altamirano MM, Calcagno ML, Garratt RC, Oliva G
Structure 7 527-37 (1999)
PMID: 10378272

Function and Biology Details

Reaction catalysed: 
Alpha-D-glucosamine 6-phosphate + H(2)O = D-fructose 6-phosphate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141540 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucosamine-6-phosphate deaminase Chain: A
Molecule details ›
Chain: A
Length: 266 amino acids
Theoretical weight: 29.81 KDa
Source organism: Escherichia coli K-12
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P6322
Unit cell:
a: 129.81Å b: 129.81Å c: 139.11Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.207 0.252
Expression system: Escherichia coli

Quick links

Citations

19 citation in other articles

Why does Escherichia coli grow more slowly on glucosamine than on N-acetylglucosamine? Effects of enzyme levels and allosteric activation of GlcN6P deaminase (NagB) on growth rates.
Alvarez-Añorve et al. (2005)
18 more

9 mentions without citation

Prediction of catalytic residues using Support Vector Machine with selected protein sequence and structural properties.
Petrova et al. (2006)
8 more