Structure of PDB 8beu Chain A

Receptor sequence
>8beuA (length=527) Species: 86832 (Rhodotorula dairenensis) [Search protein sequence]
SCAPTSLPASATELPTTVPTGTVITGDYTGSYRPQVHYSPPKGFMNAPNG
CHRDRNGTYHLYYQYNPLEYVAGNQHWGHATSDDLYHWTNQPIAIFPPNS
TSQVFSGSAVLDPNNTSGFFPNTTDGVVAVYTLNTPTLQVQEVAYSTDGG
YNFTPYENNPVLSVGSNQFRDPKVFWYEDHWVMAVAAANDFTIEIYTSPN
LTSWTFASNFTHHGLLGLAYECPNLVQVPFQDDPSKSAWLMYISINPGAP
LGGSVGQYFPGDFNGTHFVAYDSAARIADFAKDNYASQWFADTENGESIS
IAWASNWQYTQQVPTSAQAFRSAMSLPRRNYLTNITRLGWDLVSLPYDLS
PVVGPSLLSSSEANSTADVDFTNVTSNAVWFSLNVTLPDAAIQNASLISA
DASINITFLPSTKCSSSDSPAATLTYFYAGLTNGALALTRPAASSSWGAE
NPFFTDKFSYTLVDPLTSLVGVFDRSMLEVFVNEGAHSATMLVFPDSPVG
SMKVATGGLPEGTQVNLQVNGLESTWQ
3D structure
PDB8beu Insights into the Structure of the Highly Glycosylated Ffase from Rhodotorula dairenensis Enhance Its Biotechnological Potential.
ChainA
Resolution2.27 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 FRU A N187 Q205 S247 R311 D312 E362 N46 Q64 S106 R170 D171 E221
BS02 GLC A F246 E362 N387 F105 E221 N246
BS03 MAN A T157 T158 T16 T17
BS04 MAN A A150 T153 A9 T12
BS05 MAN A V159 T161 F237 V18 T20 F96
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:8beu, PDBe:8beu, PDBj:8beu
PDBsum8beu
PubMed36499311
UniProtA0A856TAI5

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