Structure of PDB 5olq Chain B

Receptor sequence
>5olqB (length=426) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
GKTYYMDPEGSDSNPGTSDKPFATLVKVQEVVVAGDVVYINPGTYVVPAN
QVPMTTTNSGLYHCVFHMNKSGEAGKPISYLANPNKQGRPIFDLSQVKPK
DQRITVFYVTGSNLYLKGFDVIGTQVTITGHTQSECFRIVKGANNNKFED
LRTHDGMAIGFYLLGGSNNHILNCDAYNNYDSVSEGGKGGNVDGFGGHIN
SSSVGEGKGTGNVFEGCRAWYNSDDGFDLINCFEAVKIINCWSFLNGYKP
GTKEVAGDGTGFKAGGYGMAADKLPAIPSVIPQHEVRNSLAYYNRLRGFY
ANHHLGGIIFESNTAVNSGENYNMTNRESPLALPPTDVNGYDHMVKNNLS
LVTRSGSKHIVMVNRAKSEVSNNSFDGSEEVIETDFISLEEAELMRDRKP
NGDLPDVNFGKLTTDAELRFWGMGCF
3D structure
PDB5olq Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides.
ChainB
Resolution1.48 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) D280 K285
Catalytic site (residue number reindexed from 1) D258 K263
Enzyme Commision number 3.2.1.22: alpha-galactosidase.
3.2.1.n1: blood group B branched chain alpha-1,3-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 CA B D215 D246 D247 D250 D193 D224 D225 D228
Gene Ontology
Molecular Function
GO:0004557 alpha-galactosidase activity
GO:0016829 lyase activity
GO:0016837 carbon-oxygen lyase activity, acting on polysaccharides
GO:0046872 metal ion binding
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:5olq, PDBe:5olq, PDBj:5olq
PDBsum5olq
PubMed29255254
UniProtQ8A051

[Back to BioLiP]