Structure of PDB 8t27 Chain A

Receptor sequence
>8t27A (length=504) Species: 837 (Porphyromonas gingivalis) [Search protein sequence]
GSHHHHHHGSMQEVTMWGDSHGVAPNQVRRTLVKVALSESLPPGAKQIRI
GFSLPKETEEKVTALYLLVSDSLAVRDLPDYKGRVSYDSFPISKEDRTTA
LSADSVAGRRFFYLAADIGPVASFSRSDTLTARVEEVAVDGRPLPLKELS
PASRRLYRGYEALFVPGDGGSRNYRIPAILKTANGTLIAMADRRKYNQTA
LPEDIDIVMRRSTDGGKSWSDPRIIVQGEGRNHGFGDVALVQTQAGKLLM
IFVGGVGLWQSTPDRPQRTYISESRDEGLTWSPPRDITHFIFGKDCADPG
RSRWLASFCASGQGLVLPSGRITFVAAIRESGQEYVLNNYVLYSDDEGDT
WQLSDCAYRRGDEAKLSLMPDGRVLMSIRNQGRQESRQRFFALSSDDGLT
WERAKQFEGIHDPGCNGAMLQVKRNGRDQVLHSLPLGPDGRRDGAVYLFD
HVSGRWSAPVVVNSGSSAYSDMTLLADGTIGYFVEEGDEISLVFIRFVLD
DLFD
3D structure
PDB8t27 Functional and structural analyses reveal that a dual domain sialidase protects bacteria from complement killing through desialylation of complement factors.
ChainA
Resolution1.41 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 SIA A R194 I195 D256 F327 D381 E382 R398 R460 Y488 R175 I176 D237 F308 D362 E363 R379 R441 Y469
BS02 GAL A Q66 D159 G160 Q47 D140 G141
BS03 GAL A G265 K266 R294 G246 K247 R275
BS04 GAL A R461 G484 S485 G506 D507 R442 G465 S466 G487 D488
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:8t27, PDBe:8t27, PDBj:8t27
PDBsum8t27
PubMed37747935
UniProtQ7MX62

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