Structure of PDB 2j78 Chain B

Receptor sequence
>2j78B (length=443) Species: 2336 (Thermotoga maritima) [Search protein sequence]
SNVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDT
GDVACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDF
YNRIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVL
FENFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRA
HARAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPL
FLNPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLV
KFDPDAAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITE
NGAAFDDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLL
DNFEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGL
3D structure
PDB2j78 Glycosidase Inhibition: An Assessment of the Binding of 18 Putative Transition-State Mimics.
ChainB
Resolution1.65 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) R77 H121 E166 V169 N293 Y295 E350
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 GOX B Q20 H121 E166 Y295 E351 W398 E405 W406 F414 Q20 H121 E166 Y295 E350 W397 E404 W405 F413 MOAD: Kd=384nM
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:2j78, PDBe:2j78, PDBj:2j78
PDBsum2j78
PubMed17279749
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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