Structure of PDB 1bgg Chain C

Receptor sequence

>1bggC (length=447) Species: 1406 (Paenibacillus polymyxa)

TIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHTPGKVFNGDNG
NVACDSYHRYEEDIRLMKELGIRTYRFSVSWPRIFPNGDGEVNQEGLDYY
HRVVDLLNDNGIEPFCTLYHWDLPQALQDAGGWGNRRTIQAFVQFAETMF
REFHGKIQHWLTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAH
GLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACARTISLHSDWFL
QPIYQGSYPQFLVDWFAEQGATVPIQDGDMDIIGEPIDMIGINYYSMSVN
RFNPEAGFLQSEEINMGLPVTDIGWPVESRGLYEVLHYLQKYGNIDIYIT
ENGACINDEVVNGKVQDDRRISYMQQHLVQVHRTIHDGLHVKGYMAWSLL
DNFEWAEGYNMRFGMIHVDFRTQVRTPKESYYWYRNVVSNNWLETRR

3D structure

• PDB: 1bgg Crystal structure of beta-glucosidase A from Bacillus polymyxa: insights into the catalytic activity in family 1 glycosyl hydrolases.
• Chain: C
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R77 H121 E166 C169 N294 Y296 E352
• Catalytic site (residue number reindexed from 1): R76 H120 E165 C168 N293 Y295 E351
• Enzyme Commision number: 3.2.1.21: beta-glucosidase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	GCO	C	Q20 H121 W122 N165 E166 Y296 W326 E352 W398 E405 W406 F414	Q19 H120 W121 N164 E165 Y295 W325 E351 W397 E404 W405 F413

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0008422 beta-glucosidase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0016052 carbohydrate catabolic process
• GO:0030245 cellulose catabolic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1bgg, PDBe:1bgg, PDBj:1bgg
• PDBsum: 1bgg
• PubMed: 9466926
• UniProt: P22073|BGLA_PAEPO Beta-glucosidase A (Gene Name=bglA)