Structure of PDB 8beu Chain D

Receptor sequence
>8beuD (length=521) Species: 86832 (Rhodotorula dairenensis) [Search protein sequence]
CAPTSLPASATELPTTVVITGDYTGSYRPQVHYSPPKGFMNAPNGCHRDR
NGTYHLYYQYNPLEYVAGNQHWGHATSDDLYHWTNQPIAIFPPNSTSQVF
SGSAVLDPNNTSGFFPNTTDGVVAVYTLNTPTLQVQEVAYSTDGGYNFTP
YENNPVLSVGSNQFRDPKVFWYEDHWVMAVAAANDFTIEIYTSPNLTSWT
FASNFTHHGLLGLAYECPNLVQVPFQDDPSKSAWLMYISINPGAPLGGSV
GQYFPGDFNGTHFVAYDSAARIADFAKDNYASQWFADTENGESISIAWAS
NWQYTQQVPTSAQAFRSAMSLPRRNYLTNITRLGWDLVSLPYDLSPVVGP
SLLSSSEANSTADVDFTNVTSNAVWFSLNVTLPDAAIQNASLISADASIN
ITFLPSTKCSSDSPAATLTYFYAGLTNGALALTRPAASSSWGAENPFFTD
KFSYTLVDPLTSLVGVFDRSMLEVFVNEGAHSATMLVFPDSPVGSMKVAT
GGLPEGTQVNLQVNGLESTWQ
3D structure
PDB8beu Insights into the Structure of the Highly Glycosylated Ffase from Rhodotorula dairenensis Enhance Its Biotechnological Potential.
ChainD
Resolution2.27 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 D N187 Q205 F246 S247 R311 D312 E362 C363 N41 Q59 F100 S101 R165 D166 E216 C217
BS02 GLC D E362 N387 E216 N241
BS03 MAN D S147 L148 P149 S5 L6 P7
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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

[Back to BioLiP]