Structure of PDB 2wbg Chain B

Receptor sequence

>2wbgB (length=443) Species: 2336 (Thermotoga maritima)

VKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGD
VACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYN
RIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLFE
NFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHA
RAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPLFL
NPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKF
DPDAPAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITEN
GAAFDDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLD
NFEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE

3D structure

• PDB: 2wbg Glycosidase Inhibition by Ring-Modified Castanospermine Analogues: Tackling Enzyme Selectivity by Inhibitor Tailoring.
• Chain: B
• Resolution: 1.85 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R77 H121 E166 V169 N293 Y295 E351
• Catalytic site (residue number reindexed from 1): R75 H119 E164 V167 N291 Y293 E349
• 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	LGS	B	Q20 H121 N165 E166 Y295 H298 W324 E351 W398 E405 W406	Q18 H119 N163 E164 Y293 H296 W322 E349 W396 E403 W404	MOAD: Ki=35.2uM

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:0030245 cellulose catabolic process

External links

• PDB: RCSB:2wbg, PDBe:2wbg, PDBj:2wbg
• PDBsum: 2wbg
• PubMed: 19532990
• UniProt: Q08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)