Structure of PDB 3lj7 Chain B

Receptor sequence
>3lj7B (length=547) Species: 10116 (Rattus norvegicus) [Search protein sequence]
TGRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQ
LVQKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQ
GLLYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVP
FVHTNVPQSMFSYDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSP
LGLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLG
PMARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYE
TDNYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSTGGLF
SDGGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAA
FLNNMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDL
NTPGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIW
DIILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQP
3D structure
PDB3lj7 Crystal structure of fatty acid amide hydrolase bound to the carbamate inhibitor URB597: discovery of a deacylating water molecule and insight into enzyme inactivation
ChainB
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) K111 S186 S187 T205 I207 G208 G209 S210 F213
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 OHO B F192 S193 I238 G239 S241 F161 S162 I207 G208 S210
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:3lj7, PDBe:3lj7, PDBj:3lj7
PDBsum3lj7
PubMed20493882
UniProtP97612|FAAH1_RAT Fatty-acid amide hydrolase 1 (Gene Name=Faah)

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