Structure of PDB 1uyq Chain A

Receptor sequence

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

TIFQFPQDFMWGTATAAYQIEGAYQEDGRGLSIWDTFAHTPGKVFNGDNG
NVACDSYHRYEEDIRLMKELGIRTYRFSVSWPRIFPNGDGEVNQEGLDYY
HRVVDLLNDNGIEPFCTLYHWDLPQALQDAGGWGNRRTIQAFVQFAETMF
REFHGKIQHWLTFNEPWCIAFLSNMLGVHAPGLTNLQTAIDVGHHLLVAH
GLSVRRFRELGTSGQIGIAPNVSWAVPYSTSEEDKAACARTISLHSDWFL
QPIYQGSYPQFLVDWFAEQGATVPIQDGDMDIIGEPIDMIGINYYSMSVN
RFNPEAGFLQSEEINMGLPVTDIGWPVESRGLYEVLHYLQKYGNIDIYIT
ENGACINDEVVNGKVQDDRRISYMQQHLVQVHRAIHDGLHVKGYMAWSLL
DNFEWAEGYNMRFGMIHVDFRTQVRTPKQSYYWYRNVVGNNWLETRR

3D structure

• PDB: 1uyq Crystal Structure of Beta-Glucosidase a from Bacillus Polymyxa: Insights Into the Catalytic Activity in Family 1 Glycosyl Hydrolases.
• Chain: A
• Resolution: 2.2 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	G2F	A	Q20 H121 N165 E166 Y296 E352 W398 E405 W406	Q19 H120 N164 E165 Y295 E351 W397 E404 W405
BS02	NFG	A	R137 Q141 V144 L203	R136 Q140 V143 L202

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:1uyq, PDBe:1uyq, PDBj:1uyq
• PDBsum: 1uyq
• UniProt: P22073|BGLA_PAEPO Beta-glucosidase A (Gene Name=bglA)