› 1fsf

X-ray diffraction
1.9Å resolution

GLUCOSAMINE-6-PHOSPHATE DEAMINASE FROM E.COLI, T CONFORMER, AT 1.9A RESOLUTION

Released:
DOI: 10.2210/pdb1fsf/pdb
PDB entry 1fsf coloured by chain, front view.
PDB entry 1fsf coloured by chain, side view.
PDB entry 1fsf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase.
Rudiño-Piñera E, Morales-Arrieta S, Rojas-Trejo SP, Horjales E
Acta Crystallogr D Biol Crystallogr 58 10-20 (2002)
PMID: 11752775

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
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 BL9-1
Spacegroup: P6322
Unit cell:
a: 126.676Å b: 126.676Å c: 139.326Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.183 0.232
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

GlobPlot: Exploring protein sequences for globularity and disorder.
Linding et al. (2003)
7 more

1 mention without citation

The tertiary origin of the allosteric activation of E. coli glucosamine-6-phosphate deaminase studied by sol-gel nanoencapsulation of its T conformer.
Zonszein et al. (2014)