Structure of PDB 5d9p Chain B

Receptor sequence
>5d9pB (length=347) Species: 77095 (Segatella bryantii) [Search protein sequence]
TYMEESAQSAVDNFGLGFNLGNTLDANGCGTGKPVATYETFWGQPETTQD
MMTFLMQNGFNAVRIPVTWYEHMDAEGNVDEAWMMRVKAIVEYAMNAGLY
AIVNVHHDTAAGSGAWIKADTDVYAATKEKFKKLWTQIANALADYDQHLL
FEGYNEMLDGNNSWDEPQKASGYEALNNYAQDFVDAVRATGGNNATRNLI
VNTYAAAKGENVLNNFMLPTDAVNNHLIVQVHSYDPWNFFNTKTTWDSEC
HNTLTEIFSALSKKFTTIPYIIGEYGTHGESDISVSKSSPAEKIKLAADQ
AADMVKLAKDHHSATFYWMSIFDGSDRIQPQWSLPTVVEAMQEAYNN
3D structure
PDB5d9p Structure-Function Analysis of a Mixed-linkage beta-Glucanase/Xyloglucanase from the Key Ruminal Bacteroidetes Prevotella bryantii B14.
ChainB
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 NBG B H112 H113 N161 E162 H238 Y240 E280 D288 W324 H106 H107 N155 E156 H232 Y234 E274 D282 W318
BS02 BGC B N28 W48 D288 N22 W42 D282
BS03 XYS B N33 W48 N27 W42
BS04 BGC B W170 W243 W164 W237
BS05 XYS B A212 A213 K214 H238 Y240 D241 A206 A207 K208 H232 Y234 D235
BS06 XYS B D241 P242 W243 D235 P236 W237
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0000272 polysaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5d9p, PDBe:5d9p, PDBj:5d9p
PDBsum5d9p
PubMed26507654
UniProtO06842

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