Structure of PDB 8j52 Chain A

Receptor sequence
>8j52A (length=510) Species: 1220578 (Flavihumibacter petaseus NBRC 106054) [Search protein sequence]
QQSLHIPLLKGECWWGAAVNRAHDMPLQPGAFIQLNGDVSGNQAVPLLLS
SAGRYVWSDQPFSVKREGDILSISFTGTGALYTASGGSLKDAWGEAAARF
FPASGRLPDTSLFTAPQYNTWIELIYNQNQEDILRYARDIVANGFPPGVL
MIDDNWFPYYGNFSFRKDRFPDAAGMISTLHGMGFKVMLWVCPFLSPDTE
AFREALAKRIVLFDSKGSDTLQWQHAVDPAIVHWWNGYSAVLDGSNPDAV
TWMREKLDGLQQQYGIDGFKFAAGDAEFYLGNILSREKIGANEQCERWGR
IGLLYPMNEYRAMWKNGGQPLVERLRDKYHTWEDVRKLIPHASLAGLLGY
SFVCPDMIGGGDFSSFKLDQELIVRSAQCHALMPMMQFSVAPWRVLDSSQ
LQAVKNAVALRRQMLPEIMKYTREAAVTGMPVLRSMEFVFPHQGFERVED
QFMLGDNYLVAPVLEKGSVRKIKLPKGRWQEIQSGKVYRGGETIELKVTL
NTIPCFKRTT
3D structure
PDB8j52 Structure-function analysis of bacterial GH31 alpha-galactosidases specific for alpha-(1→4)-galactobiose.
ChainA
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.22: alpha-galactosidase.
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 GLA A W153 D185 D186 W222 W267 K302 R343 R356 D359 W121 D153 D154 W190 W235 K270 R311 R324 D327
BS02 GAL A W267 R343 R358 D359 W235 R311 R326 D327
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016491 oxidoreductase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:8j52, PDBe:8j52, PDBj:8j52
PDBsum8j52
PubMed37438884
UniProtA0A0E9MUN5

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