Structure of PDB 1oif Chain B

Receptor sequence
>1oifB (length=442) Species: 2336 (Thermotoga maritima) [Search protein sequence]
NVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTG
DVACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFY
NRIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLF
ENFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAH
ARAVKVFRETVDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPLFL
NPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKF
DPDAAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENG
AAFDDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDN
FEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE
3D structure
PDB1oif Iminosugar Glycosidase Inhibitors: Structural and Thermodynamic Dissection of the Binding of Isofagomine and 1-Deoxynojirimycin to Beta-Glucosidases
ChainB
Resolution2.12 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 N291 Y293 E348
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 IFM B Q20 H121 E166 Y295 E351 W398 E405 W406 Q19 H120 E165 Y293 E348 W395 E402 W403 MOAD: Ka=51450000M^-1
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:1oif, PDBe:1oif, PDBj:1oif
PDBsum1oif
PubMed14624580
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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