Structure of PDB 2wj1 Chain B

Receptor sequence
>2wj1B (length=544) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLV
QKLQSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGL
LYGVPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFV
HTNVPQSMFSYDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLG
LGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPM
ARDVESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYETD
NYTMPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSTGGLFSD
GGRSFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFL
NNMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNT
PGRATGAVSYTMLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWDI
ILKKAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMTPQKQ
3D structure
PDB2wj1 Binding and Inactivation Mechanism of a Humanized Fatty Acid Amide Hydrolase by Alpha-Ketoheterocycle Inhibitors Revealed from Cocrystal Structures.
ChainB
Resolution1.84 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) K109 S184 S185 T203 I205 G206 G207 S208 F211
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 S99 B S190 M191 F192 S217 T236 D237 I238 G239 S241 C269 T488 S157 M158 F159 S184 T203 D204 I205 G206 S208 C236 T455
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:2wj1, PDBe:2wj1, PDBj:2wj1
PDBsum2wj1
PubMed19722626
UniProtP97612|FAAH1_RAT Fatty-acid amide hydrolase 1 (Gene Name=Faah)

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