Structure of PDB 8bes Chain A

Receptor sequence
>8besA (length=526) Species: 86832 (Rhodotorula dairenensis) [Search protein sequence]
SCAPTSLPASATELPTTVPTGTVITGDYTGSYRPQVHYSPPKGFMNAPNG
CHRDRNGTYHLYYQYNPLEYVAGNQHWGHATSDDLYHWTNQPIAIFPPNS
TSQVFSGSAVLDPNNTSGFFPNTTDGVVAVYTLNTPTLQVQEVAYSTDGG
YNFTPYENNPVLSVGSNQFRDPKVFWYEDHWVMAVAAANDFTIEIYTSPN
LTSWTFASNFTHHGLLGLAYECPNLVQVPFQDDPSKSAWLMYISINPGAP
LGGSVGQYFPGDFNGTHFVAYDSAARIADFAKDNYASQWFADTENGESIS
IAWASNWQYTQQVPTSAQAFRSAMSLPRRNYLTNITRLGWDLVSLPYDLS
PVVGPSLLSSSEANSTADVDFTNVTSNAVWFSLNVTLPDAAIQNASLISA
DASINITFLPSTKCSGSDSPAATLTYFYAGLTNGALALTRPAASSSWGAE
NPFFTDKFSYTLVDPLTSLVGVFDRSMLEVFVNEGAHSATMLVFPDSPVG
SMKVATGGLPEGTQVNLQVNGLESTW
3D structure
PDB8bes Insights into the Structure of the Highly Glycosylated Ffase from Rhodotorula dairenensis Enhance Its Biotechnological Potential.
ChainA
Resolution1.86 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.26: beta-fructofuranosidase.
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 MAN A T153 A458 T12 A317
BS02 MAN A V159 T161 V18 T20
BS03 FRU A N187 Q205 F246 S247 R311 D312 E362 N46 Q64 F105 S106 R170 D171 E221
BS04 MAN A G162 P233 Y292 G21 P92 Y151
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:8bes, PDBe:8bes, PDBj:8bes
PDBsum8bes
PubMed36499311
UniProtA0A856TAI5

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