Structure of PDB 5tyk Chain A

Receptor sequence
>5tykA (length=566) Species: 7375 (Lucilia cuprina) [Search protein sequence]
VSLMEKLKWKIKCIENKFLNYRLTTNETVVAETEYGKVKGVKRLTVYDDS
YYSFEGIPYAQPPVGELRFKAPQRPTPWAGVRDCCNHKDKSVQVDFITGK
VCGSEDCLYLSVYTNNLNPETKRPVLVYIHGGGFIIGENHRDMYGPDYFI
KKDVVLINIQYRLGALGFLSLNSEDLNVPGNAGLKDQVMALRWIKNNCAN
FGGNPDNITVFGESAGAASTHYMMLTEQTRGLFHRGILMSGNAICPWANT
QCQHRAFTLAKLAGYKGEDNDKDVLEFLMKAKPQDLIKLEEKVLTLEERT
NKVMFPFGPTVEPYQTADCVLPKHPREMVKTAWGNSIPTMMGNTSYEGLF
FTSILKQMPLLVKELETCVNFVPSELADAERTAPETLEMGAKIKKAHVTG
ETPTADNFMDLCSHFYFWFPMHRLLQLRFNHTSGTPVYLYRFDFDSEDLI
NPYRIMRSGRGVKGVSHTDELTYFFWNQLAKRMPKESREYKTIERMTGIW
TQFATTGNPYSNEIEGMENVSWDPIEKSDEVYKCLNISDELKMIDVPEMG
KIKQWESMFEKHRDLF
3D structure
PDB5tyk Overcoming insecticide resistance through computational inhibitor design.
ChainA
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G136 G137 G168 S218 A219 F309 F311 E351 H471
Catalytic site (residue number reindexed from 1) G132 G133 G164 S214 A215 F305 F307 E347 H467
Enzyme Commision number 3.1.1.-
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 7N4 A G136 G137 S218 A219 M308 F309 F354 F355 M460 G132 G133 S214 A215 M304 F305 F350 F351 M456 PDBbind-CN: -logKd/Ki=7.65,IC50=22.4nM
Gene Ontology
Molecular Function
GO:0017171 serine hydrolase activity
GO:0052689 carboxylic ester hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:5tyk, PDBe:5tyk, PDBj:5tyk
PDBsum5tyk
PubMed31575743
UniProtQ25252

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