› 3vus

X-ray diffraction
1.65Å resolution

Escherichia coli PgaB N-terminal domain

Released:
DOI: 10.2210/pdb3vus/pdb
PDB entry 3vus coloured by chain, front view.
PDB entry 3vus coloured by chain, side view.
PDB entry 3vus coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
The structure of the deacetylase domain of Escherichia coli PgaB, an enzyme required for biofilm formation: a circularly permuted member of the carbohydrate esterase 4 family.
Nishiyama T, Noguchi H, Yoshida H, Park SY, Tame JR
Acta Crystallogr D Biol Crystallogr 69 44-51 (2013)
PMID: 23275162

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Poly-beta-1,6-N-acetyl-D-glucosamine N-deacetylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 30.85 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P75906 (Residues: 42-309; Coverage: 41%)
Gene names: JW5142, b1023, pgaB, ycdR
Sequence domains: Polysaccharide deacetylase
Structure domains: Glycoside hydrolase/deacetylase

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand ACT 2 x ACT
Ligand HG 1 x HG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P21
Unit cell:
a: 39.559Å b: 53.114Å c: 144.17Å
α: 90° β: 95.25° γ: 90°
R-values:
R R work R free
0.206 0.205 0.256
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Chitin Deacetylases: Structures, Specificities, and Biotech Applications.
Grifoll-Romero et al. (2018)
2 more