Structure of PDB 5yqs Chain A

Receptor sequence
>5yqsA (length=754) Species: 510516 (Aspergillus oryzae RIB40) [Search protein sequence]
KPRYKDPSVPVEERVTDLLGRMTLEEKMSQLIQGDITNWMNETTGEFNLT
GLEWSTKMRGGMFYVGYPVPWDYIADNVKKAQDYILQNTTLGIPAIVQTE
SLHGFLIGNATIYNSPIGFACSFNPELIEKMARLIGQEASALGVNHVMGP
VVDLARELRFGRVEETYGEDPFLAGEIGYHYTKGIQSHNISANVKHFVGF
SQPEQGLNTAPVHGGERYLRTTWLPSFKRAIMDAGAWSIMSAYHSYDGIP
AVADYHTLTEILREEWGYKYWVTSDAGASDRVCTAFKLCRADPIDKEAVT
LAILPAGNDVEMGGGSYNFETIIDLVNAGKLDIEIVNTAVSRVLRAKFEM
GLFENPYNAAPASEWNKLIHTQEAVDLARELDRESIVLLENHDNALPLKK
SGSIAVIGPMAHGFMNYGDYVVYESQYRGVTPLDGIKAAVGDKATINYAQ
GCERWSNDQSGFAEAVEAAKKSDVAVVVVGTWSRDQKELWAGLNATTGEH
VDVNSLSLVGAQAPLIKAIIDTGVPTVVVLSSGKPITEPWLSNNTAALVQ
QFYPSEQGGNALADVLFGDYNPSGKLSVSFPHSVGDLPIYYDYLNSAREI
GDAGYIYSNGTLEFGHQYALGNPKAWYPFGYGKSYSSFEYGAVKLDKTNV
TEADTVTVSVDVKNTDATREGTEVVQVYVVDEVASVVVPNRLLKGFKKVV
IPAGQTKTVEIPLKVQDLGLWNVRMKYVVEPGAFGVLVGSSSEDIRGNAT
FYVQ
3D structure
PDB5yqs Crystal structure and substrate recognition mechanism of Aspergillus oryzae isoprimeverose-producing enzyme.
ChainA
Resolution2.4 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 3.2.1.21: beta-glucosidase.
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 BGC A E125 R187 K220 H221 Y268 D300 Y445 E524 E100 R162 K195 H196 Y243 D275 Y420 E499
BS02 XYS A Q58 Y89 G338 G339 Q33 Y64 G313 G314
BS03 GLC A N416 S659 Y660 S661 S662 N391 S634 Y635 S636 S637
BS04 XYS A E415 N416 K658 E390 N391 K633
BS05 BGC A P95 W96 N134 P70 W71 N109
BS06 CA A D706 V708 D681 V683
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
GO:0009251 glucan catabolic process
Cellular Component
GO:0005575 cellular_component

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5yqs, PDBe:5yqs, PDBj:5yqs
PDBsum5yqs
PubMed30445155
UniProtQ2U8V9

[Back to BioLiP]