Structure of PDB 3qkv Chain B Binding Site BS01

Receptor Information
>3qkv Chain B (length=543) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQ
KLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLL
YGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVH
TNVPQSMLSFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLGL
GTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPMA
RDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYETDN
YTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAGGLFSDG
GRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFLN
SMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNTP
GRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWDII
LKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQ
Ligand information
Ligand IDQKV
InChIInChI=1S/C13H16BrNO3/c14-11-1-2-12-10(7-11)8-17-13(18-12)3-5-15(9-16)6-4-13/h1-2,7,16H,3-6,8-9H2
InChIKeyVLYIBJZWDPQNBB-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370OCN1CCC2(CC1)OCc3cc(Br)ccc3O2
OpenEye OEToolkits 1.7.0c1cc2c(cc1Br)COC3(O2)CCN(CC3)CO
ACDLabs 12.01Brc2ccc1OC3(OCc1c2)CCN(CO)CC3
FormulaC13 H16 Br N O3
Name(6-bromo-1'H,4H-spiro[1,3-benzodioxine-2,4'-piperidin]-1'-yl)methanol
ChEMBL
DrugBank
ZINCZINC000066166996
PDB chain3qkv Chain B Residue 580 [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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PDB3qkv Discovery and molecular basis of potent noncovalent inhibitors of fatty acid amide hydrolase (FAAH).
Resolution3.1 Å
Binding residue
(original residue number in PDB)		L192 S193 I238 G239 S241 F381 T488
Binding residue
(residue number reindexed from 1)		L158 S159 I204 G205 S207 F347 T454
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.44,IC50=36nM
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) K108 S183 S184 T202 I204 G205 G206 S207 F210
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:3qkv, PDBe:3qkv, PDBj:3qkv
PDBsum3qkv
PubMed21502526
UniProtP97612|FAAH1_RAT Fatty-acid amide hydrolase 1 (Gene Name=Faah)

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