Structure of PDB 1mt5 Chain O Binding Site BS01

Receptor Information
>1mt5 Chain O (length=537) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEALLTLPLLQLVQKL
QSGELSPEAVFFTYLGKAWEVNKGTNCVTSYLTDCETQLSQAPRQGLLYG
VPVSLKECFSYKGHDSTLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTN
VPQSMLSFDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLGLGT
DIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQTAVQLSLGPMARD
VESLALCLKALLCEHLFTLDPTVPPLPFREEVYRSSRPLRVGYYETDNYT
MPSPAMRRALIETKQRLEAAGHTLIPFLPNNIPYALEVLSAGGLFSDGGR
SFLQNFKGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFLNSM
RPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTPMLGPALDLNTPGR
ATGAISYTVLYNCLDFPAGVVPVTTVTAEDDAQMELYKGYFGDIWDIILK
KAMKNSVGLPVAVQCVALPWQEELCLRFMREVEQLMT
Ligand information
Ligand IDMAY
InChIInChI=1S/C21H36FO2P/c1-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-18-19-20-21-25(22,23)24-2/h7-8,10-11,13-14,16-17H,3-6,9,12,15,18-21H2,1-2H3/b8-7-,11-10-,14-13-,17-16-/t25-/m0/s1
InChIKeyKWKZCGMJGHHOKJ-WTIHWRCNSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0CCCCC/C=C\C/C=C\C/C=C\C/C=C\CCCC[P@](=O)(OC)F
CACTVS 3.370CCCCCC=CCC=CCC=CCC=CCCCC[P](F)(=O)OC
OpenEye OEToolkits 1.7.0CCCCCC=CCC=CCC=CCC=CCCCCP(=O)(OC)F
CACTVS 3.370CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC[P@](F)(=O)OC
ACDLabs 12.01FP(=O)(OC)CCCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC
FormulaC21 H36 F O2 P
NameMETHYL ARACHIDONYL FLUOROPHOSPHONATE;
MAFP
ChEMBL
DrugBankDB02465
ZINCZINC000017654246
PDB chain1mt5 Chain O Residue 600 [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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PDB1mt5 Structural Adaptations in a Membrane Enzyme That Terminates Endocannabinoid Signaling
Resolution2.8 Å
Binding residue
(original residue number in PDB)		M191 L192 S193 S217 D237 I238 G239 S241 L372 A377 L380 F381 F432 T488 I491 W531
Binding residue
(residue number reindexed from 1)		M155 L156 S157 S181 D201 I202 G203 S205 L336 A341 L344 F345 F396 T452 I455 W495
Annotation score2
Binding affinityBindingDB: IC50=2.5nM
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) K106 S181 S182 T200 I202 G203 G204 S205 F208
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:1mt5, PDBe:1mt5, PDBj:1mt5
PDBsum1mt5
PubMed12459591
UniProtP97612|FAAH1_RAT Fatty-acid amide hydrolase 1 (Gene Name=Faah)

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