Structure of PDB 2j7b Chain A

Receptor sequence
>2j7bA (length=437) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGD
VACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYN
RIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLFE
NFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHA
RAVKVFRETVKDGKIGIVFNNGYFEPASEIRAVRFMHQFNNYPLFLNPIY
RGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKFDPDA
KVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENGAAFDD
VVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEWAE
GYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE
3D structure
PDB2j7b Glycosidase Inhibition: An Assessment of the Binding of 18 Putative Transition-State Mimics.
ChainA
Resolution1.87 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 N287 Y289 E343
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 NTZ A Q20 H121 N165 E166 Y295 E351 W398 E405 W406 F414 Q18 H119 N163 E164 Y289 E343 W390 E397 W398 F406 MOAD: Kd=240nM
PDBbind-CN: -logKd/Ki=6.62,Kd=240nM
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:2j7b, PDBe:2j7b, PDBj:2j7b
PDBsum2j7b
PubMed17279749
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

[Back to BioLiP]