Structure of PDB 8beq Chain B

Receptor sequence
>8beqB (length=532) Species: 86832 (Rhodotorula dairenensis) [Search protein sequence]
SCAPTSLPASATELPTTVPTGTVITGDYTGSYRPQVHYSPPKGFMNDPNG
CHRDRNGTYHLYYQYNPLEYVAGNQHWGHATSDDLYHWTNQPIAIFPPNS
TSQVFSGSAVLDPNNTSGFFPNTTDGVVAVYTLNTPTLQVQEVAYSTDGG
YNFTPYENNPVLSVGSNQFRDPKVFWYEDHWVMAVAAANDFTIEIYTSPN
LTSWTFASNFTHHGLLGLAYECPNLVQVPFQDDPSKSAWLMYISINPGAP
LGGSVGQYFPGDFNGTHFVAYDSAARIADFAKDNYASQWFADTENGESIS
IAWASNWQYTQQVPTSAQAFRSAMSLPRRNYLTNITRLGWDLVSLPYDLS
PVVGPSLLSSSEANSTADVDFTNVTSNAVWFSLNVTLPDAAIQNASLISA
DASINITFLPSTKCSSSSGSGSDSPAATLTYFYAGLTNGALALTRPAASS
SWGAENPFFTDKFSYTLVDPLTSLVGVFDRSMLEVFVNEGAHSATMLVFP
DSPVGSMKVATGGLPEGTQVNLQVNGLESTWQ
3D structure
PDB8beq Insights into the Structure of the Highly Glycosylated Ffase from Rhodotorula dairenensis Enhance Its Biotechnological Potential.
ChainB
Resolution2.07 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 B T146 S557 T5 S416
BS02 MAN B S147 L148 S6 L7
BS03 MAN B P149 S151 P8 S10
BS04 MAN B T153 S457 T12 S316
BS05 MAN B V159 T161 V18 T20
BS06 MAN B T161 T163 T20 T22
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:8beq, PDBe:8beq, PDBj:8beq
PDBsum8beq
PubMed36499311
UniProtA0A856TAI5

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