Structure of PDB 8j51 Chain B

Receptor sequence
>8j51B (length=510) Species: 1220578 (Flavihumibacter petaseus NBRC 106054) [Search protein sequence]
QQSLHIPLLKGECWWGAAVNRAHDMPLQPGAFIQLNGDVSGNQAVPLLLS
SAGRYVWSDQPFSVKREGDILSISFTGTGALYTASGGSLKDAWGEAAARF
FPASGRLPDTSLFTAPQYNTWIELIYNQNQEDILRYARDIVANGFPPGVL
MIDDNWFPYYGNFSFRKDRFPDAAGMISTLHGMGFKVMLWVCPFLSPDTE
AFREALAKRIVLFDSKGSDTLQWQHAVDPAIVHWWNGYSAVLDGSNPDAV
TWMREKLDGLQQQYGIDGFKFDAGDAEFYLGNILSREKIGANEQCERWGR
IGLLYPMNEYRAMWKNGGQPLVERLRDKYHTWEDVRKLIPHASLAGLLGY
SFVCPDMIGGGDFSSFKLDQELIVRSAQCHALMPMMQFSVAPWRVLDSSQ
LQAVKNAVALRRQMLPEIMKYTREAAVTGMPVLRSMEFVFPHQGFERVED
QFMLGDNYLVAPVLEKGSVRKIKLPKGRWQEIQSGKVYRGGETIELKVTL
NTIPCFKRTT
3D structure
PDB8j51 Structure-function analysis of bacterial GH31 alpha-galactosidases specific for alpha-(1→4)-galactobiose.
ChainB
Resolution2.15 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 B W153 D185 D186 W222 W267 K302 D304 R343 R356 D359 W121 D153 D154 W190 W235 K270 D272 R311 R324 D327
BS02 GAL B W153 D185 D186 W222 W267 K302 D304 R343 R356 D359 W121 D153 D154 W190 W235 K270 D272 R311 R324 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

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Molecular Function
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Biological Process
External links
PDB RCSB:8j51, PDBe:8j51, PDBj:8j51
PDBsum8j51
PubMed37438884
UniProtA0A0E9MUN5

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