› 2dkd

X-ray diffraction
2.1Å resolution

Crystal structure of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, in the product complex

Released:
DOI: 10.2210/pdb2dkd/pdb
PDB entry 2dkd coloured by chain, front view.
PDB entry 2dkd coloured by chain, side view.
PDB entry 2dkd coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
Crystal structures of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, and its substrate and product complexes.
Nishitani Y, Maruyama D, Nonaka T, Kita A, Fukami TA, Mio T, Yamada-Okabe H, Yamada-Okabe T, Miki K
J Biol Chem 281 19740-7 (2006)
PMID: 16651269

Function and Biology Details

Reaction catalysed: 
N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192856 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoacetylglucosamine mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 544 amino acids
Theoretical weight: 60.54 KDa
Source organism: Candida albicans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P4V2 (Residues: 1-544; Coverage: 100%)
Gene name: AGM1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NG1 2 x NG1
Ligand PO4 2 x PO4
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 60.185Å b: 129.519Å c: 81.251Å
α: 90° β: 109.22° γ: 90°
R-values:
R R work R free
0.181 0.181 0.225
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

3 mentions without citation

Biology, Mechanism, and Structure of Enzymes in the α-d-Phosphohexomutase Superfamily.
Stiers et al. (2017)
2 more