› 1ne7

X-ray diffraction
1.75Å resolution

HUMAN GLUCOSAMINE-6-PHOSPHATE DEAMINASE ISOMERASE AT 1.75 A RESOLUTION COMPLEXED WITH N-ACETYL-GLUCOSAMINE-6-PHOSPHATE AND 2-DEOXY-2-AMINO-GLUCITOL-6-PHOSPHATE

Released:
DOI: 10.2210/pdb1ne7/pdb
PDB entry 1ne7 coloured by chain, front view.
PDB entry 1ne7 coloured by chain, side view.
PDB entry 1ne7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study.
Arreola R, Valderrama B, Morante ML, Horjales E
FEBS Lett 551 63-70 (2003)
PMID: 12965206

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-155545 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glucosamine-6-phosphate deaminase 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 289 amino acids
Theoretical weight: 32.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P46926 (Residues: 1-289; Coverage: 100%)
Gene names: GNPDA1, GNPI, HLN, KIAA0060
Sequence domains: Glucosamine-6-phosphate isomerases/6-phosphogluconolactonase
Structure domains: Rossmann fold

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
3 bound ligands:
Ligand 16G 6 x 16G
Ligand SO4 7 x SO4
Ligand AGP 6 x AGP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P212121
Unit cell:
a: 109.877Å b: 110.892Å c: 180.881Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.217
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Protein O-linked β-N-acetylglucosamine: a novel effector of cardiomyocyte metabolism and function.
Darley-Usmar et al. (2012)
2 more

4 mentions without citation

Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.
Koike et al. (2009)
3 more