Structure of PDB 4ptx Chain B

Receptor sequence
>4ptxB (length=445) Species: 373903 (Halothermothrix orenii H 168) [Search protein sequence]
IIFPEDFIWGAATSSYQIEGAFNEDGKGESIWDRFSHTPGKIENGDTGDI
ACDHYHLYREDIELMKEIGIRSYRFSTSWPRILPEGKGRVNQKGLDFYKR
LVDNLLKANIRPMITLYHWDLPQALQDKGGWTNRDTAKYFAEYARLMFEE
FNGLVDLWVTHNEPWVVAFEGHAFGNHAPGTKDFKTALQVAHHLLLSHGM
AVDIFREEDLPGEIGITLNLTPAYPAGDSEKDVKAASLLDDYINAWFLSP
VFKGSYPEELHHIYEQNLGAFTTQPGDMDIISRDIDFLGINYYSRMVVRH
KPGDNLFNAEVVKMEDRPSTEMGWEIYPQGLYDILVRVNKEYTDKPLYIT
ENGAAFDDKLTEEGKIHDEKRINYLGDHFKQAYKALKDGVPLRGYYVWSL
MDNFEWAYGYSKRFGLIYVDYENGNRRFLKDSALWYREVIEKGQV
3D structure
PDB4ptx Biochemical and structural characterization of a thermostable beta-glucosidase from Halothermothrix orenii for galacto-oligosaccharide synthesis.
ChainB
Resolution1.8 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 N294 Y296 E354
Catalytic site (residue number reindexed from 1) R74 H118 E163 V166 N291 Y293 E351
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 BGC B Q20 H121 E166 Y296 E354 W401 E408 F417 Q17 H118 E163 Y293 E351 W398 E405 F414
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:0016052 carbohydrate catabolic process
GO:0030245 cellulose catabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:4ptx, PDBe:4ptx, PDBj:4ptx
PDBsum4ptx
PubMed25173693
UniProtB8CYA8

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