eF-site ID 6edw-ABCD PDB Code 6edw Chain A, B, C, D Title Crystal structure of Mycobacterium tuberculosis ICL2 in the apo form Classification LYASE Compound Isocitrate lyase 2 Source (ACEA2_MYCTO) Sequence A:  TPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQRG TIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPGQ AVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLSQ VPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDFR PFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRPG TKKXGHQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVA RTDAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLAM VRRFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFGL VSDAVNAWREDGQQSIDGIFDQVESRFVAAWEDDAGLMTY GEAVADVLEFGMAPEEWRAFAARASLHAARAKAKELGADP PWDCELAKTPEGYYQIRGGIPYAIAKSLAAAPFADILWME TKTADLADARQFAEAIHAEFPDQMLAYNLSPSFNWDTTGM TDEEMRRFPEELGKMGFVFNFITYGGHQIDGVAAEEFATA LRQDGMLALARLQRKMRLVESPYRTPQTLVGGPRSDAALA ASSGRTATTKAMSTQHQHLVQTEVPRKLLEEWLAMWSGHY QLKDKLRVQLRPQRAGSEVLELGIHGESDDKLANVIFQPI QDRRGRTILLVRDQNTFGAELRQKRLMTLIHLWLVHRFKA QAVHYVTPTDDNLYQTSKMKSHGIFTEVNQEVGEIIVAEV NHPRIAELLTPDRVALRKLITK B:  TPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQRG TIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPGQ AVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLSQ VPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDFR PFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRPG TKKXGHQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVA RTDAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLAM VRRFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFGL VSDAVNAWREDGQQSIDGIFDQVESRFVAAWEDDAGLMTY GEAVADVLEFGQSEGEPIGMAPEEWRAFAARASLHAARAK AKELGADPPWDCELAKTPEGYYQIRGGIPYAIAKSLAAAP FADILWMETKTADLADARQFAEAIHAEFPDQMLAYNLSPS FNWDTTGMTDEEMRRFPEELGKMGFVFNFITYGGHQIDGV AAEEFATALRQDGMLALARLQRKMRLVESPYRTPQTLVGG PRSDAALAASSGRTATTKAMGHLVQTEVPRKLLEEWLAMW SGHYQLKDKLRVQLRPQRAGSEVLELGIHGESDDKLANVI FQPIQDRRGRTILLVRDQNTFGAELRQKRLMTLIHLWLVH RFKAQAVHYVTPTDDNLYQTSKMKSHGIFTEVNQEVGEII VAEVNHPRIAELLTPDRVALRKLITK C:  TPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQRG TIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPGQ AVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLSQ VPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDFR PFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRPG TKKXGHQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVA RTDAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLAM VRRFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFGL VSDAVNAWREDGQQSIDGIFDQVESRFVAAWEDDAGLMTY GEAVADVLEFGQSEGEPGMAPEEWRAFAARASLHAARAKA KELGADPPWDCELAKTPEGYYQIRGGIPYAIAKSLAAAPF ADILWMETKTADLADARQFAEAIHAEFPDQMLAYNLSPSF NWDTTGMTDEEMRRFPEELGKMGFVFNFITYGGHQIDGVA AEEFATALRQDGMLALARLQRKMRLVESPYRTPQTLVGGP RSDAALAASSGRTATTKAMGVPRKLLEEWLAMWGHLRVQL RPQRAGSEVLELGIHLANVIFQPIQDRRGRTILLVRDQNT FGAELRQKRLMTLIHLWLVHRFKAQAVHYVTPTDDNLYQT SKMKSHGIFTEVNQEVGEIIVAEVNHPRIAELLTPDRVAL RKLI D:  HTPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQR GTIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPG QAVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLS QVPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDF RPFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRP GTKKXGHQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIV ARTDAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLA MVRRFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFG LVSDAVNAWREDGQQSIDGIFDQVESRFVAAWEDDAGLMT YGEAVADVLEFGQSEGEPIGMAPEEWRAFAARASLHAARA KAKELGADPPWDCELAKTPEGYYQIRGGIPYAIAKSLAAA PFADILWMETKTADLADARQFAEAIHAEFPDQMLAYNLSP SFNWDTTGMTDEEMRRFPEELGKMGFVFNFITYGGHQIDG VAAEEFATALRQDGMLALARLQRKMRLVESPYRTPQTLVG GPRSDAALAASSGRTATTKAMGEVPRKLLEEWLAMWSGHY QLKDKLRVQLRPQRAGSEVLELGIHGESDDKLANVIFQPI QDRRGRTILLVRDQNTFGALRQKRLMTLIHLWLVHRFKAQ AVHYVTPTDDNLYQTSKMKSHGIFTEVNQEVGEIIVAEVN HPRIAELLTPDRVALRKLITK Description (1)  Isocitrate lyase 2 (E.C.4.1.3.1) Functional site 1) chain A residue 17 type sequence D description binding site for residue GOL A 801 source : AC1 2) chain A residue 18 type sequence F description binding site for residue GOL A 801 source : AC1 3) chain A residue 52 type sequence T description binding site for residue GOL A 801 source : AC1 4) chain B residue 151 type sequence H description binding site for residue GOL A 801 source : AC1 5) chain A residue 151 type sequence H description binding site for residue GOL A 802 source : AC2 6) chain B residue 18 type sequence F description binding site for residue GOL A 802 source : AC2 7) chain B residue 51 type sequence G description binding site for residue GOL A 802 source : AC2 8) chain B residue 52 type sequence T description binding site for residue GOL A 802 source : AC2 9) chain A residue 450 type sequence A description binding site for residue MG A 803 source : AC3 10) chain A residue 453 type sequence A description binding site for residue MG A 803 source : AC3 11) chain A residue 482 type sequence Q description binding site for residue MG A 803 source : AC3 12) chain A residue 123 type sequence D description binding site for residue MG A 804 source : AC4 13) chain A residue 177 type sequence D description binding site for residue MG A 804 source : AC4 14) chain A residue 179 type sequence D description binding site for residue MG A 804 source : AC4 15) chain A residue 213 type sequence K description binding site for residue MG A 804 source : AC4 16) chain B residue 450 type sequence A description binding site for residue MG B 801 source : AC5 17) chain B residue 453 type sequence A description binding site for residue MG B 801 source : AC5 18) chain B residue 482 type sequence Q description binding site for residue MG B 801 source : AC5 19) chain C residue 78 type sequence R description binding site for residue GOL C 801 source : AC6 20) chain C residue 472 type sequence A description binding site for residue GOL C 801 source : AC6 21) chain C residue 476 type sequence H description binding site for residue GOL C 801 source : AC6 22) chain C residue 513 type sequence K description binding site for residue GOL C 801 source : AC6 23) chain C residue 514 type sequence M description binding site for residue GOL C 801 source : AC6 24) chain C residue 151 type sequence H description binding site for residue GOL C 802 source : AC7 25) chain D residue 18 type sequence F description binding site for residue GOL C 802 source : AC7 26) chain D residue 52 type sequence T description binding site for residue GOL C 802 source : AC7 27) chain C residue 450 type sequence A description binding site for residue MG C 803 source : AC8 28) chain C residue 453 type sequence A description binding site for residue MG C 803 source : AC8 29) chain C residue 482 type sequence Q description binding site for residue MG C 803 source : AC8 30) chain C residue 177 type sequence D description binding site for residue MG C 804 source : AC9 31) chain C residue 179 type sequence D description binding site for residue MG C 804 source : AC9 32) chain C residue 213 type sequence K description binding site for residue MG C 804 source : AC9 33) chain C residue 17 type sequence D description binding site for residue GOL D 801 source : AD1 34) chain C residue 18 type sequence F description binding site for residue GOL D 801 source : AD1 35) chain C residue 52 type sequence T description binding site for residue GOL D 801 source : AD1 36) chain D residue 151 type sequence H description binding site for residue GOL D 801 source : AD1 37) chain D residue 450 type sequence A description binding site for residue MG D 802 source : AD2 38) chain D residue 453 type sequence A description binding site for residue MG D 802 source : AD2 39) chain D residue 482 type sequence Q description binding site for residue MG D 802 source : AD2 40) chain D residue 123 type sequence D description binding site for residue MG D 803 source : AD3 41) chain D residue 177 type sequence D description binding site for residue MG D 803 source : AD3 42) chain D residue 179 type sequence D description binding site for residue MG D 803 source : AD3 43) chain D residue 213 type sequence K description binding site for residue MG D 803 source : AD3 44) chain A residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 48) chain C residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 49) chain C residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 50) chain C residue 216 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 51) chain C residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 52) chain C residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 53) chain C residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 54) chain D residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 56) chain D residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 57) chain D residue 216 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 58) chain D residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 59) chain D residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 60) chain D residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 61) chain A residue 216 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 62) chain A residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 63) chain A residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 64) chain A residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 65) chain B residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 66) chain B residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 67) chain B residue 216 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 68) chain A residue 215 type ACT_SITE sequence X description Proton acceptor => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI1 69) chain B residue 215 type ACT_SITE sequence X description Proton acceptor => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI1 70) chain C residue 215 type ACT_SITE sequence X description Proton acceptor => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI1 71) chain D residue 215 type ACT_SITE sequence X description Proton acceptor => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI1 72) chain A residue 213-218 type prosite sequence KKXGHQ description ISOCITRATE_LYASE Isocitrate lyase signature. KKCGHQ source prosite : PS00161

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