Structure of PDB 4hbp Chain B Binding Site BS01

Receptor Information
>4hbp Chain B (length=535) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQKL
QSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCAPRQGLLYGVPVSLK
ECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSML
SFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSI
RFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPMARDVESLAL
CLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYETDNYTMPSPAM
RRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAGGLFSDGGRSFLQNF
KGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFLNSMRPRSAE
KLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNTPGRATGAIS
YTVLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWDIILKKAMKNS
VGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQ
Ligand information
Ligand ID17J
InChIInChI=1S/C18H18N6OS/c25-17(20-15-7-4-8-19-13-15)23-9-11-24(12-10-23)18-21-16(22-26-18)14-5-2-1-3-6-14/h1-8,13H,9-12H2,(H,20,25)
InChIKeyRCAFZHFLIBYWGO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1ccc(cc1)c2nc(sn2)N3CCN(CC3)C(=O)Nc4cccnc4
CACTVS 3.370O=C(Nc1cccnc1)N2CCN(CC2)c3snc(n3)c4ccccc4
ACDLabs 12.01O=C(Nc1cccnc1)N4CCN(c2nc(ns2)c3ccccc3)CC4
FormulaC18 H18 N6 O S
Name4-(3-phenyl-1,2,4-thiadiazol-5-yl)-N-(pyridin-3-yl)piperazine-1-carboxamide
ChEMBLCHEMBL513553
DrugBank
ZINCZINC000035791852
PDB chain4hbp Chain B Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4hbp Synthesis, SAR study, and biological evaluation of a series of piperazine ureas as fatty acid amide hydrolase (FAAH) inhibitors.
Resolution2.91 Å
Binding residue
(original residue number in PDB)		S193 D237 I238 G239 S241 F381 M436 T488
Binding residue
(residue number reindexed from 1)		S151 D195 I196 G197 S199 F339 M394 T446
Annotation score1
Binding affinityBindingDB: IC50=8.7nM
Enzymatic activity
Catalytic site (original residue number in PDB) K142 S217 S218 T236 I238 G239 G240 S241 F244
Catalytic site (residue number reindexed from 1) K100 S175 S176 T194 I196 G197 G198 S199 F202
Enzyme Commision number 3.1.1.-
3.5.1.99: fatty acid amide hydrolase.
Gene Ontology
Molecular Function
GO:0004040 amidase activity
GO:0005515 protein binding
GO:0005543 phospholipid binding
GO:0008289 lipid binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0017064 fatty acid amide hydrolase activity
GO:0042802 identical protein binding
GO:0047372 monoacylglycerol lipase activity
Biological Process
GO:0006631 fatty acid metabolic process
GO:0009062 fatty acid catabolic process
GO:0016042 lipid catabolic process
GO:0045907 positive regulation of vasoconstriction
GO:0052651 monoacylglycerol catabolic process
GO:0150036 regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission
Cellular Component
GO:0000139 Golgi membrane
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0005794 Golgi apparatus
GO:0016020 membrane
GO:0031090 organelle membrane
GO:0098793 presynapse
GO:0098794 postsynapse
GO:0098978 glutamatergic synapse

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4hbp, PDBe:4hbp, PDBj:4hbp
PDBsum4hbp
PubMed23218778
UniProtP97612|FAAH1_RAT Fatty-acid amide hydrolase 1 (Gene Name=Faah)

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