eF-site ID 2vya-AB PDB Code 2vya Chain A, 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 A:  GRQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSE ALLTLPLLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTN CVTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHDS TLGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMF SYDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPL GLGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYG QTAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPL PFREEVYRSSRPLRVGYYETDNYTMPSPAMRRALIETKQR LEAAGHTLIPFLPNNIPYALEVLSTGGLFSDGGRSFLQNF KGDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAF LNNMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLT PMLGPALDLNTPGRATGAVSYTMLYNCLDFPAGVVPVTTV TAEDDAQMELYKGYFGDIWDIILKKAMKNSVGLPVAVQCV ALPWQEELCLRFMREVEQLMTPQ B:  RQKARGAATRARQKQRASLETMDKAVQRFRLQNPDLDSEA LLTLPLLQLVQKLQSGELSPEAVFFTYLGKAWEVNKGTNC VTSYLTDCETQLSQAPRQGLLYGVPVSLKECFSYKGHDST LGLSLNEGMPSESDCVVVQVLKLQGAVPFVHTNVPQSMFS YDCSNPLFGQTMNPWKSSKSPGGSSGGEGALIGSGGSPLG LGTDIGGSIRFPSAFCGICGLKPTGNRLSKSGLKGCVYGQ TAVQLSLGPMARDVESLALCLKALLCEHLFTLDPTVPPLP FREEVYRSSRPLRVGYYETDNYTMPSPAMRRALIETKQRL EAAGHTLIPFLPNNIPYALEVLSTGGLFSDGGRSFLQNFK GDFVDPCLGDLILILRLPSWFKRLLSLLLKPLFPRLAAFL NNMRPRSAEKLWKLQHEIEMYRQSVIAQWKAMNLDVLLTP MLGPALDLNTPGRATGAVSYTMLYNCLDFPAGVVPVTTVT AEDDAQMELYKGYFGDIWDIILKKAMKNSVGLPVAVQCVA LPWQEELCLRFMREVEQLMTP Description Functional site 1) chain A residue 259 type sequence N description BINDING SITE FOR RESIDUE CL B 1577 source : AC1 2) chain B residue 259 type sequence N description BINDING SITE FOR RESIDUE CL B 1577 source : AC1 3) chain A residue 191 type sequence M description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 4) chain A residue 192 type sequence F description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 5) chain A residue 193 type sequence S description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 6) chain A residue 194 type sequence Y description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 7) chain A residue 238 type sequence I description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 8) chain A residue 239 type sequence G description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 9) chain A residue 240 type sequence G description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 10) chain A residue 241 type sequence S description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 11) chain A residue 377 type sequence T description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 12) chain A residue 381 type sequence F description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 13) chain A residue 432 type sequence F description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 14) chain A residue 436 type sequence M description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 15) chain A residue 488 type sequence T description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 16) chain A residue 491 type sequence V description BINDING SITE FOR RESIDUE PF7 A 1578 source : AC2 17) chain B residue 191 type sequence M description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 18) chain B residue 192 type sequence F description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 19) chain B residue 193 type sequence S description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 20) chain B residue 194 type sequence Y description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 21) chain B residue 238 type sequence I description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 22) chain B residue 239 type sequence G description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 23) chain B residue 240 type sequence G description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 24) chain B residue 241 type sequence S description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 25) chain B residue 377 type sequence T description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 26) chain B residue 381 type sequence F description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 27) chain B residue 432 type sequence F description BINDING SITE FOR RESIDUE PF7 B 1578 source : AC3 28) chain A residue 142 type catalytic sequence K description 731 source MCSA : MCSA1 29) chain A residue 217 type catalytic sequence S description 731 source MCSA : MCSA1 30) chain A residue 218 type catalytic sequence S description 731 source MCSA : MCSA1 31) chain A residue 238 type catalytic sequence I description 731 source MCSA : MCSA1 32) chain A residue 239 type catalytic sequence G description 731 source MCSA : MCSA1 33) chain A residue 240 type catalytic sequence G description 731 source MCSA : MCSA1 34) chain A residue 241 type catalytic sequence S description 731 source MCSA : MCSA1 35) chain B residue 142 type catalytic sequence K description 731 source MCSA : MCSA2 36) chain B residue 217 type catalytic sequence S description 731 source MCSA : MCSA2 37) chain B residue 218 type catalytic sequence S description 731 source MCSA : MCSA2 38) chain B residue 238 type catalytic sequence I description 731 source MCSA : MCSA2 39) chain B residue 239 type catalytic sequence G description 731 source MCSA : MCSA2 40) chain B residue 240 type catalytic sequence G description 731 source MCSA : MCSA2 41) chain B residue 241 type catalytic sequence S description 731 source MCSA : MCSA2 42) chain A residue 215-246 type prosite sequence GGSSGGEGALIGSGGSPLGLGTDIGGSIRFPS description AMIDASES Amidases signature. GGSSGGeGAlIGsggsplGlGtDiGgSIRfPS source prosite : PS00571 43) chain A residue 142 type ACT_SITE sequence K description Charge relay system source Swiss-Prot : SWS_FT_FI3 44) chain A residue 217 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI3 45) chain B residue 142 type ACT_SITE sequence K description Charge relay system source Swiss-Prot : SWS_FT_FI3 46) chain B residue 217 type ACT_SITE sequence S description Charge relay system source Swiss-Prot : SWS_FT_FI3 47) chain A residue 241 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI4 48) chain B residue 241 type ACT_SITE sequence S description Acyl-ester intermediate source Swiss-Prot : SWS_FT_FI4 49) chain A residue 191 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI5 50) chain A residue 217 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 51) chain A residue 238 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI5 52) chain B residue 191 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI5 53) chain B residue 217 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI5 54) chain B residue 238 type BINDING sequence I description source Swiss-Prot : SWS_FT_FI5 55) chain A residue 404-433 type INTRAMEM sequence LILILRLPSWFKRLLSLLLKPLFPRLAAFL description INTRAMEM => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 56) chain B residue 404-433 type INTRAMEM sequence LILILRLPSWFKRLLSLLLKPLFPRLAAFL description INTRAMEM => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 57) chain A residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O00519 source Swiss-Prot : SWS_FT_FI6 58) chain B residue 241 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O00519 source Swiss-Prot : SWS_FT_FI6

Display surface Download Links