› 5b2f

X-ray diffraction
1.9Å resolution

N,N'-diacetylchitobiose deacetylase from Pyrococcus horikoshii complexed with its inhibitor MPG (phosphate-containing condition)

Released:
DOI: 10.2210/pdb5b2f/pdb
PDB entry 5b2f coloured by chain, front view.
PDB entry 5b2f coloured by chain, side view.
PDB entry 5b2f coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Substrate recognition of N,N'-diacetylchitobiose deacetylase from Pyrococcus horikoshii.
Nakamura T, Yonezawa Y, Tsuchiya Y, Niiyama M, Ida K, Oshima M, Morita J, Uegaki K
J Struct Biol 195 286-293 (2016)
PMID: 27456364

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129690 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Diacetylchitobiose deacetylase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 272 amino acids
Theoretical weight: 31.63 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58235 (Residues: 1-272; Coverage: 100%)
Gene name: PH0499
Sequence domains: GlcNAc-PI de-N-acetylase
Structure domains: LmbE-like

Ligands and Environments

2 bound ligands:
Ligand ZN 3 x ZN
Ligand MQG 3 x MQG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P3221
Unit cell:
a: 77.821Å b: 77.821Å c: 229.23Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.218 0.27
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural Insights into the Molecular Evolution of the Archaeal Exo-β-d-Glucosaminidase.
Mine et al. (2019)
4 other articles