Structure of PDB 8t1y Chain A

Receptor sequence
>8t1yA (length=493) Species: 837 (Porphyromonas gingivalis) [Search protein sequence]
QEVTMWGDSHGVAPNQVRRTLVKVALSESLPPGAKQIRIGFSLPKETEEK
VTALYLLVSDSLAVRDLPDYKGRVSYDSFPISKEDRTTALSADSVAGRRF
FYLAADIGPVASFSRSDTLTARVEEVAVDGRPLPLKELSPASRRLYRGYE
ALFVPGDGGSRNYRIPAILKTANGTLIAMADRRKYNQTDLPEDIDIVMRR
STDGGKSWSDPRIIVQGEGRNHGFGDVALVQTQAGKLLMIFVGGVGLWQS
TPDRPQRTYISESRDEGLTWSPPRDITHFIFGKDCADPGRSRWLASFCAS
GQGLVLPSGRITFVAAIRESGQEYVLNNYVLYSDDEGDTWQLSDCAYRRG
DEAKLSLMPDGRVLMSIRNQGRQESRQRFFALSSDDGLTWERAKQFEGIH
DPGCNGAMLQVKRNGRDQVLHSLPLGPDGRRDGAVYLFDHVSGRWSAPVV
VNSGSSAYSDMTLLADGTIGYFVEEGDEISLVFIRFVLDDLFD
3D structure
PDB8t1y Functional and structural analyses reveal that a dual domain sialidase protects bacteria from complement killing through desialylation of complement factors.
ChainA
Resolution2.14 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.18: exo-alpha-sialidase.
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 DAN A R194 I195 D219 D256 F327 D381 E382 R398 R460 Y488 R164 I165 D189 D226 F297 D351 E352 R368 R430 Y458
Gene Ontology
Molecular Function
GO:0004308 exo-alpha-sialidase activity
Biological Process
GO:0006689 ganglioside catabolic process
GO:0009313 oligosaccharide catabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane
GO:0043231 intracellular membrane-bounded organelle

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8t1y, PDBe:8t1y, PDBj:8t1y
PDBsum8t1y
PubMed37747935
UniProtQ7MX62

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