Structure of PDB 2j7c Chain B

Receptor sequence
>2j7cB (length=443) Species: 2336 (Thermotoga maritima) [Search protein sequence]
NVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTG
DVACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFY
NRIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLF
ENFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAH
ARAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPLF
LNPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVK
FDPDAAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITEN
GAAFDDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLD
NFEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE
3D structure
PDB2j7c Glycosidase Inhibition: An Assessment of the Binding of 18 Putative Transition-State Mimics.
ChainB
Resolution2.09 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) R76 H120 E165 V168 N292 Y294 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 IDE B Q20 H121 E166 N222 Y295 E351 W398 E405 W406 F414 Q19 H120 E165 N221 Y294 E349 W396 E403 W404 F412 MOAD: Ki=10.7nM
BS02 CA B D278 S281 E282 D277 S280 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

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2j7c, PDBe:2j7c, PDBj:2j7c
PDBsum2j7c
PubMed17279749
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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