› 2e40

X-ray diffraction
1.9Å resolution

Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium in complex with gluconolactone

Released:
DOI: 10.2210/pdb2e40/pdb
PDB entry 2e40 coloured by chain, front view.
PDB entry 2e40 coloured by chain, side view.
PDB entry 2e40 coloured by chain, top view.
Source organism: Phanerodontia chrysosporium
Primary publication:
Crystal structure of intracellular family 1 beta-glucosidase BGL1A from the basidiomycete Phanerochaete chrysosporium.
Nijikken Y, Tsukada T, Igarashi K, Samejima M, Wakagi T, Shoun H, Fushinobu S
FEBS Lett 581 1514-20 (2007)
PMID: 17376440

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173232 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucosidase 1A Chains: A, B
Molecule details ›
Chains: A, B
Length: 465 amino acids
Theoretical weight: 52.96 KDa
Source organism: Phanerodontia chrysosporium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q25BW5 (Residues: 1-462; Coverage: 100%)
Gene name: BGL1A
Sequence domains: Glycosyl hydrolase family 1
Structure domains: Glycosidases

Ligands and Environments

1 bound ligand:
Ligand LGC 2 x LGC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 65.789Å b: 120.081Å c: 133.041Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.191
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Degradation of cellulose by basidiomycetous fungi.
Baldrian et al. (2008)
3 more

5 mentions without citation

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives.
Graebin et al. (2016)
4 more