› 2vf5

X-ray diffraction
2.9Å resolution

Glucosamine-6-phosphate synthase in complex with glucosamine-6- phosphate

Released:
DOI: 10.2210/pdb2vf5/pdb
PDB entry 2vf5 coloured by chain, front view.
PDB entry 2vf5 coloured by chain, side view.
PDB entry 2vf5 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel.
Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B
J Mol Biol 377 1174-85 (2008)
PMID: 18295797

Function and Biology Details

Reaction catalysed: 
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-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-147882 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] Chain: X
Molecule details ›
Chain: X
Length: 608 amino acids
Theoretical weight: 66.85 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P17169 (Residues: 2-609; Coverage: 100%)
Gene names: JW3707, b3729, glmS
Sequence domains:
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

1 bound ligand:
Ligand GLP 1 x GLP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: R32
Unit cell:
a: 144.762Å b: 144.762Å c: 171.447Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.217 0.242
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Highlights of glucosamine-6P synthase catalysis.
Durand et al. (2008)
5 more

26 mentions without citation

Pyrazolone structural motif in medicinal chemistry: Retrospect and prospect.
Zhao et al. (2020)
25 more