Structure of PDB 6q3r Chain B

Receptor sequence
>6q3rB (length=334) Species: 5053 (Aspergillus aculeatus) [Search protein sequence]
ALTYRGADISSLLLLEDEGYSYKNLNGQTQALETILADAGINSIRQRVWV
NPSDGSYDLDYNLELAKRVKAAGMSLYLDLHLSDTWADPSDQTTPSGWST
TDLGTLKWQLYNYTLEVCNTFAENDIDIEIISIGNEIRAGLLWPLGETSS
YSNIGALLHSGAWGVKDSNLATTPKIMIHLDDGWSWDQQNYFYETVLATG
ELLSTDFDYFGVSYYPFYSASATLASLKTSLANLQSTYDKPVVVVETNWP
VSCPNPAYAFPSDLSSIPFSVAGQQEFLEKLAAVVEATTDGLGVYYWEPA
WIGNAGLGSSCADNLMVDYTTDEVYESIETLGEL
3D structure
PDB6q3r Structure of Aspergillus aculeatus beta-1,4-galactanase in complex with galactobiose.
ChainB
Resolution2.69 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R45 E136 E246
Catalytic site (residue number reindexed from 1) R45 E136 E246
Enzyme Commision number 3.2.1.89: arabinogalactan endo-beta-1,4-galactanase.
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 GAL B E136 Y218 E246 W297 L307 E136 Y218 E246 W297 L307
BS02 GAL B W86 N304 W86 N304
BS03 CA B R45 H81 N135 E246 R45 H81 N135 E246
Gene Ontology
Molecular Function
GO:0015926 glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031218 arabinogalactan endo-1,4-beta-galactosidase activity
Biological Process
GO:0045490 pectin catabolic process

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Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6q3r, PDBe:6q3r, PDBj:6q3r
PDBsum6q3r
PubMed31204685
UniProtP48842|GANA_ASPAC Arabinogalactan endo-beta-1,4-galactanase (Gene Name=gal1)

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