Structure of PDB 6fjg Chain A

Receptor sequence
>6fjgA (length=624) [Search protein sequence]
CSLDQTVAPGNLTLCGNATLFTTFRPKARFIAPEGWMNAPMGLYQRADGS
IHAGYQSHPKHIQWGNISQGAAYSSDFTSWTDFNGSEGYKTIWPSQIYDI
RGVFDGSIIKEGIDGYPTILYTSTSFGPLGATLNEAEGTETQSLAYTTDD
GASWIKLGYGAGQNPVIYEWPETNLTGFRDPYVFQSPRLEALLANTTSIT
NATGDHFATISGGVHGDGARLFLYRQHTTGEFIKWTYLGPLVTTGYKESY
GEWSGNYGINFETAGVTRLNPAGAAWDNGSDTTAVDFVTFGTEQGRADHQ
NHWPLWAAVDYEVRDNGSIEAVIAYSGVQDWGRSYAYASFPVEGYRQVSV
GWIYEDDDNVILAKQFGYQGAFTLFRDLFVKVVENVSPSTPGLFEQASWS
TKNSTDGMSVTVTTLGQRVVPETLAAYKGNSTVSTLAPVMLNESAAAYTP
FSSQPTDRFYALTGSFEFGLNTTAKAGFRVLASEEEYTDIWFDPASENLT
VVRTASSLIKSFGNDTELAKVKLYEIVGAESKTLNLTVFVDGSVIEIYAN
DEVALSTRAYPWLANSTGAGLLADGTTAGDVVGVSGLELWDGLVDAWPAR
PANTSQGLVWDGPTAAMYGLFAGY
3D structure
PDB6fjg Deciphering the molecular specificity of phenolic compounds as inhibitors or glycosyl acceptors of beta-fructofuranosidase from Xanthophyllomyces dendrorhous.
ChainA
Resolution1.73 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 N79 Q97 W105 F145 D146 R220 D221 E303 Y376 N38 Q56 W64 F104 D105 R179 D180 E262 Y335
BS02 NPO A A502 L503 T504 T578 E629 W631 A461 L462 T463 T537 E588 W590
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:6fjg, PDBe:6fjg, PDBj:6fjg
PDBsum6fjg
PubMed31767902
UniProtJ7HDY4

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