Structure of PDB 3qj9 Chain A

Receptor sequence
>3qj9A (length=549) Species: 10116 (Rattus norvegicus) [Search protein sequence]
ELETGRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLP
LLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQA
PRQGLLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQG
AVPFVHTNVPQSMLSFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSG
GSPLGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQL
SLGPMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVG
YYETDNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAG
GLFSDGGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPR
LAAFLNSMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPA
LDLNTPGRATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFG
DIWDIILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQ
3D structure
PDB3qj9 Discovery and molecular basis of potent noncovalent inhibitors of fatty acid amide hydrolase (FAAH).
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) K114 S189 S190 T208 I210 G211 G212 S213 F216
Enzyme Commision number 3.1.1.-
3.5.1.99: fatty acid amide hydrolase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 QJ9 A L192 S193 F194 I238 L404 I407 L429 M436 G485 T488 I491 W531 L164 S165 F166 I210 L376 I379 L401 M408 G457 T460 I463 W503 MOAD: ic50=951nM
PDBbind-CN: -logKd/Ki=7.00,IC50=0.10uM
BindingDB: IC50=60nM
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:3qj9, PDBe:3qj9, PDBj:3qj9
PDBsum3qj9
PubMed21502526
UniProtP97612|FAAH1_RAT Fatty-acid amide hydrolase 1 (Gene Name=Faah)

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