Structure of PDB 4tkx Chain L

Receptor sequence
>4tkxL (length=452) Species: 837 (Porphyromonas gingivalis) [Search protein sequence]
DVYTDHGDLYNTPVRMLVVAGAKFKEALKPWLTWKAQKGFYLDVHYTDEA
EVGTTNASIKAFIHKKYNDGLAASAAPVFLALVGDTDVISGEKGKKTKKV
TDLYYSAVDGDYFPEMYTFRMSASSPEELTNIIDKVLMYEKATMPDKSYL
EKVLLIAGADYSWNSQVGQPTIKYGMQYYYNQEHGYTDVYNYLKAPYTGC
YSHLNTGVSFANYTAHGSETAWADPLLTTSQLKALTNKDKYFLAIGNCCI
TAQFDYVQPCFGEVITRVKEKGAYAYIGSSPNSYWGEDYYWSVGANAVFG
VQPTFEGTSMGSYDATFLEDSYNTVNSIMWAGNLAATHAGNIGNITHIGA
HYYWEAYHVLGDGSVMPYRAMPKTNTYTLPASLPQNQASYSIQASAGSYV
AISKDGVLYGTGVANASGVATVSMTKQITENGNYDVVITRSNYLPVIKQI
QV
3D structure
PDB4tkx Structure of the lysine specific protease Kgp from Porphyromonas gingivalis, a target for improved oral health.
ChainL
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C477
Catalytic site (residue number reindexed from 1) C249
Enzyme Commision number 3.4.22.47: gingipain K.
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 TCK L A443 H444 N475 C477 S511 Y512 W513 D516 A215 H216 N247 C249 S283 Y284 W285 D288
Gene Ontology
Molecular Function
GO:0008233 peptidase activity
GO:0008234 cysteine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:4tkx, PDBe:4tkx, PDBj:4tkx
PDBsum4tkx
PubMed25327141
UniProtQ51817|KGP83_PORGN Lys-gingipain W83 (Gene Name=kgp)

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