3QJ9
Crystal structure of fatty acid amide hydrolase with small molecule inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000139 | cellular_component | Golgi membrane |
| A | 0004040 | molecular_function | amidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005543 | molecular_function | phospholipid binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005794 | cellular_component | Golgi apparatus |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0009062 | biological_process | fatty acid catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016042 | biological_process | lipid catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0017064 | molecular_function | fatty acid amide hydrolase activity |
| A | 0031090 | cellular_component | organelle membrane |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045907 | biological_process | positive regulation of vasoconstriction |
| A | 0047372 | molecular_function | monoacylglycerol lipase activity |
| A | 0052651 | biological_process | monoacylglycerol catabolic process |
| A | 0098793 | cellular_component | presynapse |
| A | 0098794 | cellular_component | postsynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0150036 | biological_process | regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0004040 | molecular_function | amidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005543 | molecular_function | phospholipid binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005794 | cellular_component | Golgi apparatus |
| B | 0006631 | biological_process | fatty acid metabolic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0009062 | biological_process | fatty acid catabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0016042 | biological_process | lipid catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0017064 | molecular_function | fatty acid amide hydrolase activity |
| B | 0031090 | cellular_component | organelle membrane |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0045907 | biological_process | positive regulation of vasoconstriction |
| B | 0047372 | molecular_function | monoacylglycerol lipase activity |
| B | 0052651 | biological_process | monoacylglycerol catabolic process |
| B | 0098793 | cellular_component | presynapse |
| B | 0098794 | cellular_component | postsynapse |
| B | 0098978 | cellular_component | glutamatergic synapse |
| B | 0150036 | biological_process | regulation of trans-synaptic signaling by endocannabinoid, modulating synaptic transmission |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE QJ9 A 600 |
| Chain | Residue |
| A | LEU192 |
| A | LEU429 |
| A | GLY485 |
| A | THR488 |
| A | ILE491 |
| A | HOH806 |
| A | SER193 |
| A | PHE194 |
| A | ILE238 |
| A | GLY239 |
| A | SER241 |
| A | PHE381 |
| A | LEU404 |
| A | ILE407 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 580 |
| Chain | Residue |
| A | GLU288 |
| A | LYS295 |
| A | GLU316 |
| A | ARG320 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 581 |
| Chain | Residue |
| A | ARG34 |
| A | PHE396 |
| A | VAL397 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 582 |
| Chain | Residue |
| A | ARG437 |
| A | PRO438 |
| A | ARG439 |
| A | LYS443 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 583 |
| Chain | Residue |
| A | ASN108 |
| A | LYS109 |
| A | ASN112 |
| A | HOH631 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 584 |
| Chain | Residue |
| A | LYS446 |
| A | HIS449 |
| B | GLU515 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 585 |
| Chain | Residue |
| A | TYR329 |
| A | GLU331 |
| A | LYS350 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 586 |
| Chain | Residue |
| A | ALA275 |
| A | VAL276 |
| A | GLN277 |
| A | ILE451 |
| A | ASN498 |
| A | CYS499 |
| A | ASP501 |
| A | HOH628 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 587 |
| Chain | Residue |
| A | THR42 |
| A | HOH889 |
| B | ARG323 |
| B | HOH812 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 588 |
| Chain | Residue |
| A | GLN46 |
| A | LYS47 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PGE A 589 |
| Chain | Residue |
| A | LEU75 |
| A | THR76 |
| A | GLY226 |
| A | GLY250 |
| A | ILE251 |
| A | ARG285 |
| A | HOH597 |
| A | HOH772 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 590 |
| Chain | Residue |
| A | VAL509 |
| A | THR510 |
| site_id | BC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE QJ9 B 600 |
| Chain | Residue |
| B | LEU192 |
| B | SER193 |
| B | PHE194 |
| B | ILE238 |
| B | GLY239 |
| B | PHE381 |
| B | LEU404 |
| B | ILE407 |
| B | LEU429 |
| B | GLY485 |
| B | THR488 |
| B | ILE491 |
| B | EDO583 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 580 |
| Chain | Residue |
| B | LYS47 |
| B | GLN48 |
| B | SER51 |
| B | THR115 |
| B | SER116 |
| B | PHE201 |
| B | HOH735 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 581 |
| Chain | Residue |
| B | TYR330 |
| B | ASP333 |
| B | ILE368 |
| B | SER492 |
| B | TYR493 |
| B | LEU496 |
| B | TYR497 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 582 |
| Chain | Residue |
| B | GLU288 |
| B | LEU292 |
| B | LYS295 |
| B | GLU316 |
| B | ARG320 |
| B | HOH751 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 583 |
| Chain | Residue |
| B | SER193 |
| B | PHE194 |
| B | PRO484 |
| B | GLY485 |
| B | QJ9600 |
| B | HOH733 |
| B | HOH787 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 584 |
| Chain | Residue |
| B | THR76 |
| B | LEU77 |
| B | GLN81 |
| B | HOH621 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 585 |
| Chain | Residue |
| B | THR511 |
| B | THR573 |
| B | HOH694 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 586 |
| Chain | Residue |
| B | ARG343 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 587 |
| Chain | Residue |
| B | PRO78 |
| B | LEU80 |
| B | GLN81 |
| B | HOH755 |
| B | HOH955 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 588 |
| Chain | Residue |
| B | ARG45 |
| B | PHE396 |
| B | HOH728 |
| B | HOH869 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 589 |
| Chain | Residue |
| B | ARG344 |
| B | THR513 |
| B | GLU515 |
| B | ASP516 |
| B | HOH838 |
| site_id | CC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO B 590 |
| Chain | Residue |
| B | TYR370 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 591 |
| Chain | Residue |
| B | ARG352 |
| B | LEU571 |
| site_id | CC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 592 |
| Chain | Residue |
| B | MET191 |
| B | HOH931 |
Functional Information from PROSITE/UniProt
| site_id | PS00571 |
| Number of Residues | 32 |
| Details | AMIDASES Amidases signature. GGSSGGeGAlIGsggsplGlGtDiGgSIRfPS |
| Chain | Residue | Details |
| A | GLY215-SER246 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 58 |
| Details | INTRAMEM: INTRAMEM => ECO:0000305 |
| Chain | Residue | Details |
| A | LEU404-LEU433 | |
| B | LEU404-LEU433 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 290 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | ASN434-SER579 | |
| B | ASN434-SER579 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| A | LYS142 | |
| A | SER217 | |
| B | LYS142 | |
| B | SER217 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | ACT_SITE: Acyl-ester intermediate |
| Chain | Residue | Details |
| A | SER241 | |
| B | SER241 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | MET191 | |
| A | SER217 | |
| A | ILE238 | |
| B | MET191 | |
| B | SER217 | |
| B | ILE238 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O00519 |
| Chain | Residue | Details |
| A | SER241 | |
| B | SER241 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 731 |
| Chain | Residue | Details |
| A | LYS142 | proton acceptor, proton donor |
| A | SER217 | proton acceptor, proton donor, proton relay |
| A | SER218 | electrostatic stabiliser |
| A | ILE238 | electrostatic stabiliser |
| A | GLY239 | electrostatic stabiliser |
| A | GLY240 | electrostatic stabiliser |
| A | SER241 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 731 |
| Chain | Residue | Details |
| B | LYS142 | proton acceptor, proton donor |
| B | SER217 | proton acceptor, proton donor, proton relay |
| B | SER218 | electrostatic stabiliser |
| B | ILE238 | electrostatic stabiliser |
| B | GLY239 | electrostatic stabiliser |
| B | GLY240 | electrostatic stabiliser |
| B | SER241 | nucleofuge, nucleophile, proton acceptor, proton donor |
