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BioLiP

Structure of PDB 2cbu Chain A

Receptor sequence
>2cbuA (length=440) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGD
VACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYN
RIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLFE
NFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHA
RAVKVFRETVKDGKIGIVFNNGYFEPASEKDIRAVRFMHQFNNYPLFLNP
IYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKFDP
DAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENGAAF
DDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEW
AEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLED
3D structure
PDB2cbu Dissection of Conformationally Restricted Inhibitors Binding to a Beta-Glucosidase.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 N289 Y291 E345
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 A Q20 H121 N165 E166 Y295 W324 E351 W398 E405 W406 F414 Q18 H119 N163 E164 Y291 W318 E345 W392 E399 W400 F408 MOAD: Kd=2.1uM
PDBbind-CN: -logKd/Ki=5.68,Kd=2.1uM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2cbu, PDBe:2cbu, PDBj:2cbu
PDBsum2cbu
PubMed16628756
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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