› 2vhl

X-ray diffraction
2.05Å resolution

The Three-dimensional structure of the N-Acetylglucosamine-6- phosphate deacetylase from Bacillus subtilis

Released:
DOI: 10.2210/pdb2vhl/pdb
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Source organism: Bacillus subtilis
Primary publication:
The three-dimensional structure of the N-acetylglucosamine-6-phosphate deacetylase, NagA, from Bacillus subtilis: a member of the urease superfamily.
Vincent F, Yates D, Garman E, Davies GJ, Brannigan JA
J Biol Chem 279 2809-16 (2004)
PMID: 14557261

Function and Biology Details

Reaction catalysed: 
N-acetyl-D-glucosamine 6-phosphate + H(2)O = D-glucosamine 6-phosphate + acetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128538 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylglucosamine-6-phosphate deacetylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 396 amino acids
Theoretical weight: 42.67 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O34450 (Residues: 1-396; Coverage: 100%)
Gene names: BSU35010, nagA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GLP 2 x GLP
Ligand PGE 2 x PGE
Ligand FE 4 x FE
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21212
Unit cell:
a: 51.68Å b: 107.74Å c: 188.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.26
Expression system: Escherichia coli

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Citations

2 review citations

Recent structural insights into the expanding world of carbohydrate-active enzymes.
Davies et al. (2005)
1 more

5 mentions without citation

Structural and chemical biology of deacetylases for carbohydrates, proteins, small molecules and histones.
Bürger et al. (2018)
4 more

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