Structure of PDB 8bes Chain D

Receptor sequence
>8besD (length=524) Species: 86832 (Rhodotorula dairenensis) [Search protein sequence]
CAPTSLPASATELPTTVPTGTVITGDYTGSYRPQVHYSPPKGFMNAPNGC
HRDRNGTYHLYYQYNPLEYVAGNQHWGHATSDDLYHWTNQPIAIFPPNST
SQVFSGSAVLDPNNTSGFFPNTTDGVVAVYTLNTPTLQVQEVAYSTDGGY
NFTPYENNPVLSVGSNQFRDPKVFWYEDHWVMAVAAANDFTIEIYTSPNL
TSWTFASNFTHHGLLGLAYECPNLVQVPFQDDPSKSAWLMYISINPGAPL
GGSVGQYFPGDFNGTHFVAYDSAARIADFAKDNYASQWFADTENGESISI
AWASNWQYTQQVPTSAQAFRSAMSLPRRNYLTNITRLGWDLVSLPYDLSP
VVGPSLLSSSEANSTADVDFTNVTSNAVWFSLNVTLPDAAIQNASLISAD
ASINITFLPSTKCSSDSPAATLTYFYAGLTNGALALTRPAASSSWGAENP
FFTDKFSYTLVDPLTSLVGVFDRSMLEVFVNEGAHSATMLVFPDSPVGSM
KVATGGLPEGTQVNLQVNGLESTW
3D structure
PDB8bes Insights into the Structure of the Highly Glycosylated Ffase from Rhodotorula dairenensis Enhance Its Biotechnological Potential.
ChainD
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 D P149 S151 P7 S9
BS02 MAN D T153 A458 T11 A316
BS03 FRU D N187 Q205 F246 S247 R311 D312 E362 W448 N45 Q63 F104 S105 R169 D170 E220 W306
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
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Biological Process
External links
PDB RCSB:8bes, PDBe:8bes, PDBj:8bes
PDBsum8bes
PubMed36499311
UniProtA0A856TAI5

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