Structure of PDB 2vrj Chain B

Receptor sequence
>2vrjB (length=443) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGD
VACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYN
RIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLFE
NFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHA
RAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPLFL
NPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKF
DPDAPAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITEN
GAAFDDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLD
NFEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE
3D structure
PDB2vrj Molecular Basis for Beta-Glucosidase Inhibition by Ring-Modified Calystegine Analogues.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 NCW B Q20 E166 Y177 Y295 E351 W398 E405 W406 Q18 E164 Y175 Y293 E349 W396 E403 W404 MOAD: Kd=0.5uM
BS02 CA B D278 E282 D276 E280
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2vrj, PDBe:2vrj, PDBj:2vrj
PDBsum2vrj
PubMed18833549
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

[Back to BioLiP]