eF-site ID 1iyx-AB PDB Code 1iyx Chain A, B click to enlarge Title Crystal structure of enolase from Enterococcus hirae Classification LYASE Compound ENOLASE Source ORGANISM_SCIENTIFIC: Enterococcus hirae; Sequence A:  SIITDVYAREILDSRGNPTIEVEVYTESGAFGRGMVPSGA STGEYEAVELRDGDKARYGGKGVTKAVDNVNNIIAEAIIG YDVRDQMAIDKAMIALDGTPNKGKLGANAILGVSIAVARA AADYLEVPLYHYLGGFNTKVLPTPMMNIINGGSHADNSID FQEFMIMPVGAPTFKEALRMGAEVFHALAAILKSRGLATS VGDEGGFAPNLGSNEEGFEVIIEAIEKAGYVPGKDVVLAM DAASSEFYDKEKGVYVLADSGEGEKTTDEMIKFYEELVSK YPIISIEDGLDENDWDGFKKLTDVLGDKVQLVGDDLFVTN TQKLSEGIEKGIANSILIKVNQIGTLTETFEAIEMAKEAG YTAVVSHRSGETEDSTISDIAVATNAGQIKTGSLSRTDRI AKYNQLLRIEDQLGEVAEYKGLKSFYNLKAA B:  SIITDVYAREILDSRGNPTIEVEVYTESGAFGRGMVPSGA STGEYEAVELRDGDKARYGGKGVTKAVDNVNNIIAEAIIG YDVRDQMAIDKAMIALDGTPNKGKLGANAILGVSIAVARA AADYLEVPLYHYLGGFNTKVLPTPMMNIINGGSHADNSID FQEFMIMPVGAPTFKEALRMGAEVFHALAAILKSRGLATS VGDEGGFAPNLGSNEEGFEVIIEAIEKAGYVPGKDVVLAM DAASSEFYDKEKGVYVLADSGEGEKTTDEMIKFYEELVSK YPIISIEDGLDENDWDGFKKLTDVLGDKVQLVGDDLFVTN TQKLSEGIEKGIANSILIKVNQIGTLTETFEAIEMAKEAG YTAVVSHRSGETEDSTISDIAVATNAGQIKTGSLSRTDRI AKYNQLLRIEDQLGEVAEYKGLKSFYNLKAA Description Functional site 1) chain A residue 162 type sequence Q description BINDING SITE FOR RESIDUE MG A 1432 source : AC1 2) chain A residue 241 type sequence D description BINDING SITE FOR RESIDUE MG A 1432 source : AC1 3) chain A residue 287 type sequence E description BINDING SITE FOR RESIDUE MG A 1432 source : AC1 4) chain A residue 390 type sequence K description BINDING SITE FOR RESIDUE MG A 1432 source : AC1 5) chain B residue 241 type sequence D description BINDING SITE FOR RESIDUE MG B 1432 source : AC2 6) chain B residue 287 type sequence E description BINDING SITE FOR RESIDUE MG B 1432 source : AC2 7) chain B residue 288 type sequence D description BINDING SITE FOR RESIDUE MG B 1432 source : AC2 8) chain B residue 314 type sequence D description BINDING SITE FOR RESIDUE MG B 1432 source : AC2 9) chain B residue 39 type sequence G description BINDING SITE FOR RESIDUE SO4 B 1001 source : AC3 10) chain B residue 40 type sequence A description BINDING SITE FOR RESIDUE SO4 B 1001 source : AC3 11) chain B residue 339 type sequence K description BINDING SITE FOR RESIDUE SO4 B 1001 source : AC3 12) chain B residue 368 type sequence R description BINDING SITE FOR RESIDUE SO4 B 1001 source : AC3 13) chain B residue 369 type sequence S description BINDING SITE FOR RESIDUE SO4 B 1001 source : AC3 14) chain A residue 339 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC4 15) chain A residue 368 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC4 16) chain A residue 369 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC4 17) chain A residue 411 type sequence D description BINDING SITE FOR RESIDUE GOL A 2001 source : AC5 18) chain B residue 7 type sequence Y description BINDING SITE FOR RESIDUE GOL A 2001 source : AC5 19) chain A residue 5 type sequence D description BINDING SITE FOR RESIDUE GOL A 2002 source : AC6 20) chain A residue 7 type sequence Y description BINDING SITE FOR RESIDUE GOL A 2002 source : AC6 21) chain A residue 25 type sequence Y description BINDING SITE FOR RESIDUE GOL A 2002 source : AC6 22) chain A residue 77 type sequence A description BINDING SITE FOR RESIDUE GOL A 2003 source : AC7 23) chain A residue 79 type sequence I description BINDING SITE FOR RESIDUE GOL A 2003 source : AC7 24) chain B residue 77 type sequence A description BINDING SITE FOR RESIDUE GOL B 2004 source : AC8 25) chain B residue 79 type sequence I description BINDING SITE FOR RESIDUE GOL B 2004 source : AC8 26) chain B residue 81 type sequence Y description BINDING SITE FOR RESIDUE GOL B 2004 source : AC8 27) chain A residue 87 type sequence M description BINDING SITE FOR RESIDUE GOL A 2005 source : AC9 28) chain A residue 348 type sequence E description BINDING SITE FOR RESIDUE GOL A 2005 source : AC9 29) chain A residue 351 type sequence E description BINDING SITE FOR RESIDUE GOL A 2005 source : AC9 30) chain A residue 125 type sequence L description BINDING SITE FOR RESIDUE GOL B 2006 source : BC1 31) chain A residue 131 type sequence H description BINDING SITE FOR RESIDUE GOL B 2006 source : BC1 32) chain A residue 132 type sequence Y description BINDING SITE FOR RESIDUE GOL B 2006 source : BC1 33) chain B residue 125 type sequence L description BINDING SITE FOR RESIDUE GOL B 2006 source : BC1 34) chain B residue 131 type sequence H description BINDING SITE FOR RESIDUE GOL B 2006 source : BC1 35) chain B residue 135 type sequence G description BINDING SITE FOR RESIDUE GOL B 2006 source : BC1 36) chain A residue 154 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 37) chain B residue 314 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 366 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 39) chain B residue 390 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 163 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 287 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 42) chain A residue 314 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 366 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 44) chain A residue 390 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 45) chain B residue 154 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 163 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 47) chain B residue 287 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 204 type ACT_SITE sequence E description Proton donor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI1 49) chain B residue 204 type ACT_SITE sequence E description Proton donor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 339 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 339 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 241 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 53) chain B residue 241 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI4 54) chain A residue 339 type BINDING sequence K description covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI5 55) chain B residue 339 type BINDING sequence K description covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI5 56) chain A residue 336-349 type prosite sequence ILIKVNQIGTLTET description ENOLASE Enolase signature. ILIKvNQIGTLTET source prosite : PS00164

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