eF-site ID 6o4n-AB PDB Code 6o4n Chain A, B click to enlarge Title Crystal Structure of Enolase from Chlamydia trachomatis Classification HYDROLASE Compound Enolase Source (ENO_CHLTB) Sequence A:  DVVISDIEAREILDSRGYPTLCVKVITNTGTFGEACVPSG ASTGIKEALELRDKDPKRYQGKGVLQAISNVEKVLVPALQ GFSVFDQITADAIMIDADGTPNKEKLGANAILGVSLALAK AAANTLQRPLYRYLGGSFSHVLPCPMMNLINGGMHATNGL QFQEFMIRPISAPSLKEAVRMGAEVFNALKKILQNRQLAT GVGDEGGFAPNLASNAEALDLLLTAIETAGFTPREDISLA LDCAASSFYNTQDKTYDGKSYADQVGILAELCEHYPIDSI EDGLAEEDFEGWKLLSETLGDRVQLVGDDLFVTNSALIAE GIAQGLANAVLIKPNQIGTLTETAEAIRLATIQGYATILS HRSGETEDTTIADLAVAFNTGQIKTGSLSRSERIAKYNRL MAIEEEMGPEALFQDSNPFSKA B:  DVVISDIEAREILDSRGYPTLCVKVITNTGTFGEACVPSG ASTGIKEALELRDKDPKRYQGKGVLQAISNVEKVLVPALQ GFSVFDQITADAIMIDADGTPNKEKLGANAILGVSLALAK AAANTLQRPLYRYLGGSFSHVLPCPMMNLINGGMHATNGL QFQEFMIRPISAPSLKEAVRMGAEVFNALKKILQNRQLAT GVGDEGGFAPNLASNAEALDLLLTAIETAGFTPREDISLA LDCAASSFYNTQDKTYDGKSYADQVGILAELCEHYPIDSI EDGLAEEDFEGWKLLSETLGDRVQLVGDDLFVTNSALIAE GIAQGLANAVLIKPNQIGTLTETAEAIRLATIQGYATILS HRSGETEDTTIADLAVAFNTGQIKTGSLSRSERIAKYNRL MAIEEEMGPEALFQDSNPFSKA Description Functional site 1) chain A residue 48 type sequence K description binding site for residue MRD A 501 source : AC1 2) chain A residue 289 type sequence E description binding site for residue MRD A 501 source : AC1 3) chain A residue 291 type sequence F description binding site for residue MRD A 501 source : AC1 4) chain A residue 312 type sequence L description binding site for residue MRD A 501 source : AC1 5) chain A residue 319 type sequence L description binding site for residue MRD A 501 source : AC1 6) chain A residue 322 type sequence E description binding site for residue MRD A 501 source : AC1 7) chain A residue 326 type sequence Q description binding site for residue MRD A 501 source : AC1 8) chain A residue 56 type sequence K description binding site for residue EDO A 502 source : AC2 9) chain A residue 63 type sequence G description binding site for residue EDO A 502 source : AC2 10) chain A residue 68 type sequence Q description binding site for residue EDO A 503 source : AC3 11) chain A residue 42 type sequence G description binding site for residue PO4 A 504 source : AC4 12) chain A residue 43 type sequence A description binding site for residue PO4 A 504 source : AC4 13) chain A residue 44 type sequence S description binding site for residue PO4 A 504 source : AC4 14) chain A residue 157 type sequence H description binding site for residue PO4 A 504 source : AC4 15) chain A residue 165 type sequence Q description binding site for residue PO4 A 504 source : AC4 16) chain A residue 335 type sequence K description binding site for residue PO4 A 504 source : AC4 17) chain A residue 364 type sequence R description binding site for residue PO4 A 504 source : AC4 18) chain A residue 365 type sequence S description binding site for residue PO4 A 504 source : AC4 19) chain A residue 44 type sequence S description binding site for residue MG A 505 source : AC5 20) chain A residue 244 type sequence D description binding site for residue MG A 506 source : AC6 21) chain A residue 283 type sequence E description binding site for residue MG A 506 source : AC6 22) chain A residue 310 type sequence D description binding site for residue MG A 506 source : AC6 23) chain A residue 335 type sequence K description binding site for residue MG A 506 source : AC6 24) chain A residue 386 type sequence K description binding site for residue MG A 506 source : AC6 25) chain A residue 12 type sequence R description binding site for residue MRD A 507 source : AC7 26) chain A residue 36 type sequence E description binding site for residue MRD A 507 source : AC7 27) chain A residue 38 type sequence C description binding site for residue MRD A 507 source : AC7 28) chain A residue 369 type sequence E description binding site for residue MRD A 507 source : AC7 29) chain A residue 370 type sequence D description binding site for residue MRD A 507 source : AC7 30) chain A residue 101 type sequence G description binding site for residue EDO A 508 source : AC8 31) chain A residue 102 type sequence T description binding site for residue EDO A 508 source : AC8 32) chain A residue 357 type sequence Y description binding site for residue EDO A 509 source : AC9 33) chain A residue 163 type sequence Q description binding site for residue EDO A 510 source : AD1 34) chain A residue 216 type sequence S description binding site for residue EDO A 510 source : AD1 35) chain A residue 217 type sequence N description binding site for residue EDO A 510 source : AD1 36) chain A residue 45 type sequence T description binding site for residue MG A 511 source : AD2 37) chain A residue 201 type sequence A description binding site for residue CL A 512 source : AD3 38) chain A residue 213 type sequence N description binding site for residue CL A 512 source : AD3 39) chain A residue 213 type sequence N description binding site for residue EDO A 513 source : AD4 40) chain B residue 199 type sequence Q description binding site for residue EDO A 513 source : AD4 41) chain B residue 201 type sequence A description binding site for residue EDO A 513 source : AD4 42) chain A residue 199 type sequence Q description binding site for residue EDO B 1601 source : AD5 43) chain A residue 200 type sequence L description binding site for residue EDO B 1601 source : AD5 44) chain A residue 201 type sequence A description binding site for residue EDO B 1601 source : AD5 45) chain B residue 213 type sequence N description binding site for residue EDO B 1601 source : AD5 46) chain B residue 289 type sequence E description binding site for residue MRD B 1602 source : AD6 47) chain B residue 291 type sequence F description binding site for residue MRD B 1602 source : AD6 48) chain B residue 312 type sequence L description binding site for residue MRD B 1602 source : AD6 49) chain B residue 319 type sequence L description binding site for residue MRD B 1602 source : AD6 50) chain B residue 322 type sequence E description binding site for residue MRD B 1602 source : AD6 51) chain B residue 42 type sequence G description binding site for residue PO4 B 1603 source : AD7 52) chain B residue 43 type sequence A description binding site for residue PO4 B 1603 source : AD7 53) chain B residue 44 type sequence S description binding site for residue PO4 B 1603 source : AD7 54) chain B residue 157 type sequence H description binding site for residue PO4 B 1603 source : AD7 55) chain B residue 165 type sequence Q description binding site for residue PO4 B 1603 source : AD7 56) chain B residue 335 type sequence K description binding site for residue PO4 B 1603 source : AD7 57) chain B residue 364 type sequence R description binding site for residue PO4 B 1603 source : AD7 58) chain B residue 365 type sequence S description binding site for residue PO4 B 1603 source : AD7 59) chain B residue 44 type sequence S description binding site for residue MG B 1604 source : AD8 60) chain B residue 244 type sequence D description binding site for residue MG B 1605 source : AD9 61) chain B residue 283 type sequence E description binding site for residue MG B 1605 source : AD9 62) chain B residue 310 type sequence D description binding site for residue MG B 1605 source : AD9 63) chain B residue 335 type sequence K description binding site for residue MG B 1605 source : AD9 64) chain B residue 386 type sequence K description binding site for residue MG B 1605 source : AD9 65) chain B residue 12 type sequence R description binding site for residue MRD B 1606 source : AE1 66) chain B residue 36 type sequence E description binding site for residue MRD B 1606 source : AE1 67) chain B residue 38 type sequence C description binding site for residue MRD B 1606 source : AE1 68) chain B residue 122 type sequence K description binding site for residue MRD B 1606 source : AE1 69) chain B residue 369 type sequence E description binding site for residue MRD B 1606 source : AE1 70) chain B residue 370 type sequence D description binding site for residue MRD B 1606 source : AE1 71) chain B residue 68 type sequence Q description binding site for residue EDO B 1607 source : AE2 72) chain A residue 157 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 73) chain B residue 244 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 74) chain B residue 283 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 310 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 76) chain B residue 362 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 77) chain B residue 386 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 78) chain A residue 166 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 79) chain A residue 244 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 80) chain A residue 283 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 81) chain A residue 310 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 82) chain A residue 362 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 83) chain A residue 386 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 84) chain B residue 157 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 85) chain B residue 166 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI3 86) chain A residue 207 type ACT_SITE sequence E description Proton donor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI1 87) chain B residue 207 type ACT_SITE sequence E description Proton donor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI1 88) chain A residue 335 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI2 89) chain B residue 335 type ACT_SITE sequence K description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI2 90) chain A residue 335 type BINDING sequence K description covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI4 91) chain B residue 335 type BINDING sequence K description covalent; in inhibited form => ECO:0000255|HAMAP-Rule:MF_00318 source Swiss-Prot : SWS_FT_FI4 92) chain A residue 332-345 type prosite sequence VLIKPNQIGTLTET description ENOLASE Enolase signature. VLIKpNQIGTLTET source prosite : PS00164

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