Structure of PDB 3pr0 Chain B Binding Site BS01

Receptor Information
>3pr0 Chain B (length=548) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
WTGRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLL
QLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPR
QGLLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAV
PFVHTNVPQSMFSYDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGS
PLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSL
GPMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYY
ETDNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSTGGL
FSDGGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLA
AFLNNMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALD
LNTPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDI
WDIILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQP
Ligand information
Ligand IDJG2
InChIInChI=1S/C20H23N3O3/c24-20(25,14-8-2-1-4-10-16-11-5-3-6-12-16)19-23-22-18(26-19)17-13-7-9-15-21-17/h3,5-7,9,11-13,15,24-25H,1-2,4,8,10,14H2
InChIKeyKSJFCWCEVWDLIS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370OC(O)(CCCCCCc1ccccc1)c2oc(nn2)c3ccccn3
OpenEye OEToolkits 1.7.2c1ccc(cc1)CCCCCCC(c2nnc(o2)c3ccccn3)(O)O
ACDLabs 12.01n3c(c1nnc(o1)C(O)(O)CCCCCCc2ccccc2)cccc3
FormulaC20 H23 N3 O3
Name7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptane-1,1-diol;
7-phenyl-1-[5-(pyridin-2-yl)-1,3,4-oxadiazol-2-yl]heptan-1-one, bound form
ChEMBL
DrugBank
ZINCZINC000098209045
PDB chain3pr0 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

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3pr0 Fluoride-mediated capture of a noncovalent bound state of a reversible covalent enzyme inhibitor: X-ray crystallographic analysis of an exceptionally potent alpha-ketoheterocycle inhibitor of fatty acid amide hydrolase.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		K142 M191 F192 S217 D237 I238 G239 S241 C269 T488
Binding residue
(residue number reindexed from 1)		K112 M161 F162 S187 D207 I208 G209 S211 C239 T458
Annotation score1
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) K112 S187 S188 T206 I208 G209 G210 S211 F214
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3pr0, PDBe:3pr0, PDBj:3pr0
PDBsum3pr0
PubMed21355555
UniProtP97612|FAAH1_RAT Fatty-acid amide hydrolase 1 (Gene Name=Faah)

[Back to BioLiP]