Structure of PDB 2jal Chain A

Receptor sequence
>2jalA (length=436) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGD
VACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYN
RIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLFE
NFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHA
RAVKVFRETVKDGKIGIVFNNGYFEPASERAVRFMHQFNNYPLFLNPIYR
GDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKFDPDAK
VSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENGAAFDDV
VSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEWAEG
YSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE
3D structure
PDB2jal Structural Basis for Cyclophellitol Inhibition of a Beta-Glucosidase.
ChainA
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 N286 Y288 E342
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 YLL A Q20 H121 E166 E351 W398 E405 W406 F414 Q18 H119 E164 E342 W389 E396 W397 F405 PDBbind-CN: -logKd/Ki=4.82,Ki=15uM
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:2jal, PDBe:2jal, PDBj:2jal
PDBsum2jal
PubMed17252125
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

[Back to BioLiP]