› 2put

X-ray diffraction
1.9Å resolution

The crystal structure of isomerase domain of glucosamine-6-phosphate synthase from Candida albicans

Released:
DOI: 10.2210/pdb2put/pdb
PDB entry 2put coloured by chain, front view.
PDB entry 2put coloured by chain, side view.
PDB entry 2put coloured by chain, top view.
Source organism: Candida albicans SC5314
Primary publication:
The crystal and solution studies of glucosamine-6-phosphate synthase from Candida albicans.
Raczynska J, Olchowy J, Konariev PV, Svergun DI, Milewski S, Rypniewski W
J Mol Biol 372 672-88 (2007)
PMID: 17681543

Function and Biology Details

Reaction catalysed: 
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156861 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 367 amino acids
Theoretical weight: 40.61 KDa
Source organism: Candida albicans SC5314
Expression system: Escherichia coli
UniProt:
  • Canonical: P53704 (Residues: 347-713; Coverage: 52%)
Gene names: CAALFM_C302280CA, CaO19.1618, GFA1
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

4 bound ligands:
Ligand ACT 2 x ACT
Ligand NA 4 x NA
Ligand UD1 4 x UD1
Ligand F6R 4 x F6R
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 66.028Å b: 118.188Å c: 100.032Å
α: 90° β: 91.78° γ: 90°
R-values:
R R work R free
0.172 0.171 0.215
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
5 more

1 mention without citation

Properties of Cavities in Biological Structures-A Survey of the Protein Data Bank.
Chwastyk et al. (2020)