Structure of PDB 4l2l Chain A Binding Site BS02

Receptor Information
>4l2l Chain A (length=607) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLV
LDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIE
ISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVK
LTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIA
LVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVW
GQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTG
NLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSV
KTFGETHPFTKLVVDLTDIDPDVAYSSVPYEKGFALLFYLEQLLGGPEIF
LGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGL
PPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFL
AQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPL
ALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLV
GKDLKVD
Ligand information
Ligand ID1V6
InChIInChI=1S/C16H14N2S/c17-16-18-15(11-19-16)14-8-6-13(7-9-14)10-12-4-2-1-3-5-12/h1-9,11H,10H2,(H2,17,18)
InChIKeyXYDVHKCVOMGRSY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1ccc(cc1)Cc2ccc(cc2)c3csc(n3)N
ACDLabs 12.01n3c(c1ccc(cc1)Cc2ccccc2)csc3N
CACTVS 3.370Nc1scc(n1)c2ccc(Cc3ccccc3)cc2
FormulaC16 H14 N2 S
Name4-(4-benzylphenyl)-1,3-thiazol-2-amine
ChEMBLCHEMBL3883608
DrugBank
ZINCZINC000003722646
PDB chain4l2l Chain A Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4l2l Binding of Pro-Gly-Pro at the active site of leukotriene A4 hydrolase/aminopeptidase and development of an epoxide hydrolase selective inhibitor.
Resolution1.648 Å
Binding residue
(original residue number in PDB)		Q136 A137 Y267 W311 F314 F362 K364 L365 V367 P374 A377 Y378 P382
Binding residue
(residue number reindexed from 1)		Q133 A134 Y264 W308 F311 F359 K361 L362 V364 P371 A374 Y375 P379
Annotation score1
Binding affinityMOAD: Ki=2.3uM
PDBbind-CN: -logKd/Ki=5.70,Ki=0.002mM
BindingDB: IC50=12400nM,Kd=130nM,Ki=360nM
Enzymatic activity
Catalytic site (original residue number in PDB) E271 H295 E296 H299 E318 D375 Y383
Catalytic site (residue number reindexed from 1) E268 H292 E293 H296 E315 D372 Y380
Enzyme Commision number 3.3.2.6: leukotriene-A4 hydrolase.
3.4.11.4: tripeptide aminopeptidase.
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0004177 aminopeptidase activity
GO:0004301 epoxide hydrolase activity
GO:0004463 leukotriene-A4 hydrolase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0045148 tripeptide aminopeptidase activity
GO:0046872 metal ion binding
GO:0070006 metalloaminopeptidase activity
Biological Process
GO:0006508 proteolysis
GO:0006629 lipid metabolic process
GO:0006691 leukotriene metabolic process
GO:0010043 response to zinc ion
GO:0019370 leukotriene biosynthetic process
GO:0019538 protein metabolic process
GO:0043171 peptide catabolic process
GO:0043434 response to peptide hormone
GO:0060509 type I pneumocyte differentiation
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0070062 extracellular exosome
GO:1904724 tertiary granule lumen
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4l2l, PDBe:4l2l, PDBj:4l2l
PDBsum4l2l
PubMed24591641
UniProtP09960|LKHA4_HUMAN Leukotriene A-4 hydrolase (Gene Name=LTA4H)

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