Structure of PDB 5n6s Chain D

Receptor sequence
>5n6sD (length=431) Species: 2336 (Thermotoga maritima) [Search protein sequence]
VKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGD
VACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYN
RIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLFE
NFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHA
RAVKVFRETVKDGKIGIVFNNGYFEPASEKEDIRAVRFMHQFNNYPLFLN
PIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKFD
PDAPAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENG
AAFDDVVRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEWA
EGYSKRFGIVYVDYSTQVKYWYSNVVKNNGL
3D structure
PDB5n6s Carba-cyclophellitols Are Neutral Retaining-Glucosidase Inhibitors.
ChainD
Resolution2.1 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) R75 H119 E164 V167 N290 Y292 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 8P5 D Q20 H121 E166 Y295 E351 W398 E405 Q18 H119 E164 Y292 E348 W391 E398
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:5n6s, PDBe:5n6s, PDBj:5n6s
PDBsum5n6s
PubMed28463498
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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