Structure of PDB 4j5p Chain A Binding Site BS01

Receptor Information
>4j5p Chain A (length=544) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQL
VQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQG
LLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPF
VHTNVPQSMFSYDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPL
GLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGP
MARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYET
DNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSTGGLFS
DGGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAF
LNNMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLN
TPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWD
IILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQK
Ligand information
Ligand IDBR1
InChIInChI=1S/C22H25BrN2O2/c23-14-18-12-13-19(24-15-18)21-16-25-22(27-21)20(26)11-7-2-1-4-8-17-9-5-3-6-10-17/h3,5-6,9-10,12-13,15-16,20,26H,1-2,4,7-8,11,14H2/t20-/m0/s1
InChIKeyLMYCIAKTMGFSLZ-FQEVSTJZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6c1ccc(cc1)CCCCCCC(c2ncc(o2)c3ccc(cn3)CBr)O
ACDLabs 12.01BrCc1ccc(nc1)c2oc(nc2)C(O)CCCCCCc3ccccc3
CACTVS 3.370O[CH](CCCCCCc1ccccc1)c2oc(cn2)c3ccc(CBr)cn3
OpenEye OEToolkits 1.7.6c1ccc(cc1)CCCCCC[C@@H](c2ncc(o2)c3ccc(cn3)CBr)O
CACTVS 3.370O[C@@H](CCCCCCc1ccccc1)c2oc(cn2)c3ccc(CBr)cn3
FormulaC22 H25 Br N2 O2
Name(1S)-1-{5-[5-(bromomethyl)pyridin-2-yl]-1,3-oxazol-2-yl}-7-phenylheptan-1-ol;
1-(5-(5-(bromomethyl)pyridin-2-yl)-7-phenylheptan-1-one, bound form
ChEMBL
DrugBank
ZINCZINC000098208705
PDB chain4j5p Chain A Residue 601 [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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PDB4j5p Rational design of Fatty Acid amide hydrolase inhibitors that act by covalently bonding to two active site residues.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		S190 M191 F192 S193 S217 T236 D237 I238 G239 G240 S241 C269 F432 T488
Binding residue
(residue number reindexed from 1)		S158 M159 F160 S161 S185 T204 D205 I206 G207 G208 S209 C237 F400 T456
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=7.92,Ki=12nM
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) K110 S185 S186 T204 I206 G207 G208 S209 F212
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:4j5p, PDBe:4j5p, PDBj:4j5p
PDBsum4j5p
PubMed23581831
UniProtP97612|FAAH1_RAT Fatty-acid amide hydrolase 1 (Gene Name=Faah)

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