› 5gzk

X-ray diffraction
1.7Å resolution

Endo-beta-1,2-glucanase from Chitinophaga pinensis - sophorotriose and glucose complex

Released:
DOI: 10.2210/pdb5gzk/pdb
PDB entry 5gzk coloured by chain, front view.
PDB entry 5gzk coloured by chain, side view.
PDB entry 5gzk coloured by chain, top view.
Source organism: Chitinophaga pinensis DSM 2588
Primary publication:
Biochemical and structural analyses of a bacterial endo-β-1,2-glucanase reveal a new glycoside hydrolase family.
Abe K, Nakajima M, Yamashita T, Matsunaga H, Kamisuki S, Nihira T, Takahashi Y, Sugimoto N, Miyanaga A, Nakai H, Arakawa T, Fushinobu S, Taguchi H
J Biol Chem 292 7487-7506 (2017)
PMID: 28270506

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165710 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Uncharacterized protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 461 amino acids
Theoretical weight: 52.39 KDa
Source organism: Chitinophaga pinensis DSM 2588
Expression system: Escherichia coli BL21(DE3)
Structure domains: Glycosyltransferase

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC
Carbohydrate polymer
7 bound ligands:
Ligand PO4 2 x PO4
Ligand K 2 x K
Ligand BGC 2 x BGC
Ligand PG4 1 x PG4
Ligand PEG 1 x PEG
Ligand CL 1 x CL
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: C2
Unit cell:
a: 126.106Å b: 117.401Å c: 75.554Å
α: 90° β: 92.56° γ: 90°
R-values:
R R work R free
0.168 0.166 0.199
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Cyclic β-glucans at the bacteria-host cells interphase: One sugar ring to rule them all.
Guidolin et al. (2018)
10 other articles

4 mentions without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)
3 more