Structure of PDB 5olr Chain B

Receptor sequence
>5olrB (length=425) Species: 818 (Bacteroides thetaiotaomicron) [Search protein sequence]
KTYYMDPEGSDSNPGTSDKPFATLVKVQEVVVAGDVVYINPGTYVVPANQ
VPMTTTNSGLYHCVFHMNKSGEAGKPISYLANPNKQGRPIFDLSQVKPKD
QRITVFYVTGSNLYLKGFDVIGTQVTITGHTQSECFRIVKGANNNKFEDL
RTHDGMAIGFYLLGGSNNHILNCDAYNNYDSVSEGGKGGNVDGFGGHINS
SSVGEGKGTGNVFEGCRAWYNSDDGFDLINCFEAVKIINCWSFLNGYKPG
TKEVAGDGTGFKAGGYGMAADKLPAIPSVIPQHEVRNSLAYYNRLRGFYA
NHHLGGIIFESNTAVNSGENYNMTNRESPLALPPTDVNGYDHMVKNNLSL
VTRSGSKHIVMVNRAKSEVSNNSFDGSEEVIETDFISLEEAELMRDRKPN
GDLPDVNFGKLTTDAELRFWGMGCF
3D structure
PDB5olr Dietary pectic glycans are degraded by coordinated enzyme pathways in human colonic Bacteroides.
ChainB
Resolution1.07 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D280 K285
Catalytic site (residue number reindexed from 1) D257 K262
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 RAM B H153 Q155 Y184 H220 H130 Q132 Y161 H197
BS02 ADA B R125 H153 R102 H130
BS03 CA B G212 D246 D280 G189 D223 D257
BS04 CA B D215 D246 D247 D250 D192 D223 D224 D227
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

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Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:5olr, PDBe:5olr, PDBj:5olr
PDBsum5olr
PubMed29255254
UniProtQ8A051

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