Structure of PDB 5tyn Chain A

Receptor sequence
>5tynA (length=568) Species: 7375 (Lucilia cuprina) [Search protein sequence]
FNVSLMEKLKWKIKCIENKFLNYRLTTNETVVAETEYGKVKGVKRLTVYD
DSYYSFEGIPYAQPPVGELRFKAPQRPTPWAGVRDCCNHKDKSVQVDFIT
GKVCGSEDCLYLSVYTNNLNPETKRPVLVYIHGGGFIIGENHRDMYGPDY
FIKKDVVLINIQYRLGALGFLSLNSEDLNVPGNAGLKDQVMALRWIKNNC
ANFGGNPDNITVFGESAGAASTHYMMLTEQTRGLFHRGILMSGNAICPWA
NTQCQHRAFTLAKLAGYKGEDNDKDVLEFLMKAKPQDLIKLEEKVLTLEE
RTNKVMFPFGPTVEPYQTADCVLPKHPREMVKTAWGNSIPTMMGNTSYEG
LFFTSILKQMPLLVKELETCVNFVPSELADAERTAPETLEMGAKIKKAHV
TGETPTADNFMDLCSHFYFWFPMHRLLQLRFNHTSGTPVYLYRFDFDSED
LINPYRIMRSGRGVKGVSHTDELTYFFWNQLAKRMPKESREYKTIERMTG
IWTQFATTGNPYSNEIEGMENVSWDPIEKSDEVYKCLNISDELKMIDVPE
MGKIKQWESMFEKHRDLF
3D structure
PDB5tyn Overcoming insecticide resistance through computational inhibitor design.
ChainA
Resolution1.531 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) G134 G135 G166 S216 A217 F307 F309 E349 H469
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 7NS A G135 G136 G137 S218 A219 W251 M308 F309 F354 G133 G134 G135 S216 A217 W249 M306 F307 F352 PDBbind-CN: -logKd/Ki=9.28,IC50=0.52nM
Gene Ontology
Molecular Function
GO:0017171 serine hydrolase activity
GO:0052689 carboxylic ester hydrolase activity

View graph for
Molecular Function
External links
PDB RCSB:5tyn, PDBe:5tyn, PDBj:5tyn
PDBsum5tyn
PubMed31575743
UniProtQ25252

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