Structure of PDB 2cbu Chain B

Receptor sequence

>2cbuB (length=441) Species: 2336 (Thermotoga maritima)

NVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTG
DVACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFY
NRIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLF
ENFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAH
ARAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPLF
LNPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVK
FDPDAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENG
AAFDDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDN
FEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGL

3D structure

• PDB: 2cbu Dissection of Conformationally Restricted Inhibitors Binding to a Beta-Glucosidase.
• 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): R76 H120 E165 V168 N292 Y294 E348
• 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	CTS	B	Q20 H121 W122 N165 E166 Y295 W324 E351 W398 E405 W406 F414	Q19 H120 W121 N164 E165 Y294 W321 E348 W395 E402 W403 F411	MOAD: Kd=2.1uM
BS02	CA	B	D278 E282	D277 E281

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:2cbu, PDBe:2cbu, PDBj:2cbu
• PDBsum: 2cbu
• PubMed: 16628756
• UniProt: Q08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)