eF-site ID 3puh-AB PDB Code 3puh Chain A, B click to enlarge Title Cocaine Esterase, wild-type biologically active dimer Classification HYDROLASE Compound Cocaine esterase Source Rhodococcus sp. (strain MB1 Bresler) (COCE_RHOSM) Sequence A:  GNYSVASNVMVPMRDGVRLAVDLYRPDADGPVPVLLVRNP YDKFDVFAWSTQSTNWLEFVRDGYAVVIQDTRGLFASEGE FVPHVDDEADAEDTLSWILEQAWCDGNVGMFGVSYLGVTQ WQAAVSGVGGLKAIAPSMASADLYRAPWYGPGGALSVEAL LGWSALIGTGLITSRSDARPEDAADFVQLAAILNDVAGAA SVTPLAEQPLLGRLIPWVIDQVVDHPDNDESWQSISLFER LGGLATPALITAGWYDGFVGESLRTFVAVKDNADARLVVG PWSHSNLTGRNADRKFGIAATYPIQEATTMHKAFFDRHLR GETDALAGVPKVRLFVMGIDEWRDETDWPLPDTAYTPFYL GGSGAANTSTGGGTLSTSISGTESADTYLYDPADPVPSLG GTLLFHNGDNGPADQRPIHDRDDVLCYSTEVLTDPVEVTG TVSARLFVSSSAVDTDFTAKLVDVFPDGRAIALCDGIVRM RYRETLVNPTLIEAGEIYEVAIDMLATSNVFLPGHRIMVQ VSSSNFPKYDRNSNTGGVIAREQLEEMCTAVNRIHRGPEH PSHIVLPIIKR B:  MVDGNYSVASNVMVPMRDGVRLAVDLYRPDADGPVPVLLV RNPYDKFDVFAWSTQSTNWLEFVRDGYAVVIQDTRGLFAS EGEFVPHVDDEADAEDTLSWILEQAWCDGNVGMFGVSYLG VTQWQAAVSGVGGLKAIAPSMASADLYRAPWYGPGGALSV EALLGWSALIGTGLITSRSDARPEDAADFVQLAAILNDVA GAASVTPLAEQPLLGRLIPWVIDQVVDHPDNDESWQSISL FERLGGLATPALITAGWYDGFVGESLRTFVAVKDNADARL VVGPWSHSNLTGRNADRKFGIAATYPIQEATTMHKAFFDR HLRGETDALAGVPKVRLFVMGIDEWRDETDWPLPDTAYTP FYLGGSGAANTSTGGGTLSTSISGTESADTYLYDPADPVP SLGGTLLFHNGDNGPADQRPIHDRDDVLCYSTEVLTDPVE VTGTVSARLFVSSSAVDTDFTAKLVDVFPDGRAIALCDGI VRMRYRETLVNPTLIEAGEIYEVAIDMLATSNVFLPGHRI MVQVSSSNFPKYDRNSNTGGVIAREQLEEMCTAVNRIHRG PEHPSHIVLPIIKR Description Functional site 1) chain A residue 197 type sequence N description BINDING SITE FOR RESIDUE GOL A 588 source : AC1 2) chain A residue 199 type sequence V description BINDING SITE FOR RESIDUE GOL A 588 source : AC1 3) chain A residue 408 type sequence F description BINDING SITE FOR RESIDUE GOL A 588 source : AC1 4) chain A residue 409 type sequence H description BINDING SITE FOR RESIDUE GOL A 588 source : AC1 5) chain A residue 410 type sequence N description BINDING SITE FOR RESIDUE GOL A 588 source : AC1 6) chain B residue 293 type sequence R description BINDING SITE FOR RESIDUE GOL A 588 source : AC1 7) chain B residue 298 type sequence K description BINDING SITE FOR RESIDUE GOL A 588 source : AC1 8) chain A residue 554 type sequence V description BINDING SITE FOR RESIDUE GOL A 589 source : AC2 9) chain A residue 556 type sequence R description BINDING SITE FOR RESIDUE GOL A 589 source : AC2 10) chain B residue 452 type sequence S description BINDING SITE FOR RESIDUE GOL A 589 source : AC2 11) chain B residue 454 type sequence S description BINDING SITE FOR RESIDUE GOL A 589 source : AC2 12) chain B residue 554 type sequence V description BINDING SITE FOR RESIDUE GOL A 589 source : AC2 13) chain B residue 103 type sequence E description BINDING SITE FOR RESIDUE SO4 A 590 source : AC3 14) chain A residue 296 type sequence D description BINDING SITE FOR RESIDUE SO4 A 591 source : AC4 15) chain B residue 296 type sequence D description BINDING SITE FOR RESIDUE SO4 A 591 source : AC4 16) chain A residue 319 type sequence D description BINDING SITE FOR RESIDUE SO4 A 592 source : AC5 17) chain A residue 323 type sequence R description BINDING SITE FOR RESIDUE SO4 A 592 source : AC5 18) chain A residue 325 type sequence E description BINDING SITE FOR RESIDUE SO4 A 592 source : AC5 19) chain A residue 293 type sequence R description BINDING SITE FOR RESIDUE GOL B 588 source : AC6 20) chain A residue 298 type sequence K description BINDING SITE FOR RESIDUE GOL B 588 source : AC6 21) chain B residue 196 type sequence L description BINDING SITE FOR RESIDUE GOL B 588 source : AC6 22) chain B residue 199 type sequence V description BINDING SITE FOR RESIDUE GOL B 588 source : AC6 23) chain B residue 408 type sequence F description BINDING SITE FOR RESIDUE GOL B 588 source : AC6 24) chain B residue 409 type sequence H description BINDING SITE FOR RESIDUE GOL B 588 source : AC6 25) chain B residue 410 type sequence N description BINDING SITE FOR RESIDUE GOL B 588 source : AC6 26) chain B residue 65 type sequence D description BINDING SITE FOR RESIDUE SO4 B 589 source : AC7 27) chain B residue 319 type sequence D description BINDING SITE FOR RESIDUE SO4 B 589 source : AC7 28) chain B residue 325 type sequence E description BINDING SITE FOR RESIDUE SO4 B 589 source : AC7 29) chain A residue 44 type catalytic sequence Y description 465 source MCSA : MCSA1 30) chain A residue 117 type catalytic sequence S description 465 source MCSA : MCSA1 31) chain A residue 118 type catalytic sequence Y description 465 source MCSA : MCSA1 32) chain A residue 166 type catalytic sequence W description 465 source MCSA : MCSA1 33) chain A residue 259 type catalytic sequence D description 465 source MCSA : MCSA1 34) chain A residue 287 type catalytic sequence H description 465 source MCSA : MCSA1 35) chain B residue 44 type catalytic sequence Y description 465 source MCSA : MCSA2 36) chain B residue 117 type catalytic sequence S description 465 source MCSA : MCSA2 37) chain B residue 118 type catalytic sequence Y description 465 source MCSA : MCSA2 38) chain B residue 166 type catalytic sequence W description 465 source MCSA : MCSA2 39) chain B residue 259 type catalytic sequence D description 465 source MCSA : MCSA2 40) chain B residue 287 type catalytic sequence H description 465 source MCSA : MCSA2 41) chain A residue 117 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000269|PubMed:11742345 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 117 type ACT_SITE sequence S description Acyl-ester intermediate => ECO:0000269|PubMed:11742345 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 259 type ACT_SITE sequence D description Charge relay system => ECO:0000269|PubMed:11742345 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 287 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:11742345 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 259 type ACT_SITE sequence D description Charge relay system => ECO:0000269|PubMed:11742345 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 287 type ACT_SITE sequence H description Charge relay system => ECO:0000269|PubMed:11742345 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 44 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 48) chain A residue 118 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 49) chain B residue 44 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 50) chain B residue 118 type BINDING sequence Y description source Swiss-Prot : SWS_FT_FI3 51) chain A residue 44 type SITE sequence Y description Probably involved in activating the substrate carbonyl and the acyl enzyme for hydrolysis source Swiss-Prot : SWS_FT_FI4 52) chain B residue 44 type SITE sequence Y description Probably involved in activating the substrate carbonyl and the acyl enzyme for hydrolysis source Swiss-Prot : SWS_FT_FI4

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