Structure of PDB 5n6s Chain C

Receptor sequence
>5n6sC (length=428) Species: 2336 (Thermotoga maritima) [Search protein sequence]
KKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGDV
ACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYNR
IIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLFEN
FGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHAR
AVKVFRETDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPLFLNPI
YRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKFDPD
APAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENGAA
FDDRVHDQNRDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEWAEGYSK
RFGIVYVDYSVKDSGYWYSNVVKNNGLE
3D structure
PDB5n6s Carba-cyclophellitols Are Neutral Retaining-Glucosidase Inhibitors.
ChainC
Resolution2.1 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) R74 H118 E163 V166 N288 Y290 E346
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 8P5 C Q20 H121 E166 Y295 E351 W398 E405 F414 Q17 H118 E163 Y290 E346 W386 E393 F402
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:5n6s, PDBe:5n6s, PDBj:5n6s
PDBsum5n6s
PubMed28463498
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

[Back to BioLiP]