› 5ns6

X-ray diffraction
1.5Å resolution

Crystal structure of beta-glucosidase BglM-G1 from marine metagenome

Released:
DOI: 10.2210/pdb5ns6/pdb
PDB entry 5ns6 coloured by chain, front view.
PDB entry 5ns6 coloured by chain, side view.
PDB entry 5ns6 coloured by chain, top view.
Source organism: marine metagenome
Primary publication:
Loss of a conserved salt bridge in bacterial glycosyl hydrolase BgIM-G1 improves substrate binding in temperate environments.
Mhaindarkar D, Gasper R, Lupilov N, Hofmann E, Leichert LI
OpenAccess logo Commun Biol 1 171 (2018)
PMID: 30345395

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166033 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 455 amino acids
Theoretical weight: 51.88 KDa
Source organism: marine metagenome
Expression system: Not provided
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand SO4 11 x SO4
Ligand GOL 23 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P43
Unit cell:
a: 138.02Å b: 138.02Å c: 97.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.172
Expression system: Not provided

Quick links

Citations

3 citation in other articles

Less Unfavorable Salt Bridges on the Enzyme Surface Result in More Organic Cosolvent Resistance.
Cui et al. (2021)
2 more

1 mention without citation

Loss of a conserved salt bridge in bacterial glycosyl hydrolase BgIM-G1 improves substrate binding in temperate environments.
Mhaindarkar et al. (2018)