Structure of PDB 8t26 Chain A

Receptor sequence
>8t26A (length=504) Species: 837 (Porphyromonas gingivalis) [Search protein sequence]
GSHHHHHHGSMQEVTMWGDSHGVAPNQVRRTLVKVALSESLPPGAKQIRI
GFSLPKETEEKVTALYLLVSDSLAVRDLPDYKGRVSYDSFPISKEDRTTA
LSADSVAGRRFFYLAADIGPVASFSRSDTLTARVEEVAVDGRPLPLKELS
PASRRLYRGYEALFVPGDGGSRNYRIPAILKTANGTLIAMADRRKYNQTA
LPEDIDIVMRRSTDGGKSWSDPRIIVQGEGRNHGFGDVALVQTQAGKLLM
IFVGGVGLWQSTPDRPQRTYISESRDEGLTWSPPRDITHFIFGKDCADPG
RSRWLASFCASGQGLVLPSGRITFVAAIRESGQEYVLNNYVLYSDDEGDT
WQLSDCAYRRGDEAKLSLMPDGRVLMSIRNQGRQESRQRFFALSSDDGLT
WERAKQFEGIHDPGCNGAMLQVKRNGRDQVLHSLPLGPDGRRDGAVYLFD
HVSGRWSAPVVVNSGSSAYSDMTLLADGTIGYFVEEGDEISLVFIRFVLD
DLFD
3D structure
PDB8t26 Functional and structural analyses reveal that a dual domain sialidase protects bacteria from complement killing through desialylation of complement factors.
ChainA
Resolution1.42 Å
3D
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
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
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:8t26, PDBe:8t26, PDBj:8t26
PDBsum8t26
PubMed37747935
UniProtQ7MX62

[Back to BioLiP]