eF-site ID 2vya-B PDB Code 2vya Chain B click to enlarge Title Crystal Structure of fatty acid amide hydrolase conjugated with the drug-like inhibitor PF-750 Classification HYDROLASE Compound FATTY-ACID AMIDE HYDROLASE 1 Source Rattus norvegicus (Rat) (FAAH1_RAT) Sequence B:  RQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEA LLTLPLLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNC VTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHDST LGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMFS YDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLG LGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQ TAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPLP FREEVYRSSRPLRVGYYETDNYTMPSPAMRRALIETKQRL EAAGHTLIPFLPNNIPYALEVLSTGGLFSDGGRSFLQNFK GDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFL NNMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTP MLGPALDLNTPGRATGAVSYTMLYNCLDFPAGVVPVTTVT AEDDAQMELYKGYFGDIWDIILKKAMKNSVGLPVAVQCVA LPWQEELCLRFMREVEQLMTP Description Functional site 1) chain B residue 259 type sequence N description BINDING SITE FOR RESIDUE CL B 1577 source : AC1 2) chain B residue 191 type sequence M description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 3) chain B residue 192 type sequence F description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 4) chain B residue 193 type sequence S description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 5) chain B residue 194 type sequence Y description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 6) chain B residue 238 type sequence I description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 7) chain B residue 239 type sequence G description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 8) chain B residue 240 type sequence G description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 9) chain B residue 241 type sequence S description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 10) chain B residue 377 type sequence T description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 11) chain B residue 381 type sequence F description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 12) chain B residue 432 type sequence F description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 13) chain B residue 142 type catalytic sequence K description 731 source MCSA : MCSA2 14) chain B residue 217 type catalytic sequence S description 731 source MCSA : MCSA2 15) chain B residue 218 type catalytic sequence S description 731 source MCSA : MCSA2 16) chain B residue 238 type catalytic sequence I description 731 source MCSA : MCSA2 17) chain B residue 239 type catalytic sequence G description 731 source MCSA : MCSA2 18) chain B residue 240 type catalytic sequence G description 731 source MCSA : MCSA2 19) chain B residue 241 type catalytic sequence S description 731 source MCSA : MCSA2 20) chain B residue 404-433 type INTRAMEM sequence LILILRLPSWFKRLLSLLLKPLFPRLAAFL description INTRAMEM => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 142 type ACT_SITE sequence K description Charge relay system source Swiss-Prot : SWS_FT_FI3 22) chain B residue 217 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI3 23) chain B residue 241 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI4 24) chain B residue 191 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI5 25) chain B residue 217 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 26) chain B residue 238 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI5 27) chain B residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O00519 source Swiss-Prot : SWS_FT_FI6

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