eF-site ID 6edz-ABCD PDB Code 6edz Chain A, B, C, D click to enlarge Title Crystal structure of Mycobacterium tuberculosis ICL2 in complex with acetyl-CoA, form I Classification LYASE Compound Isocitrate lyase 2 Source (ACEA2_MYCTO) Sequence A:  TPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQRG TIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPGQ AVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLSQ VPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDFR PFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRPG TKKXGHQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVA RTDAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLAM VRRFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFGL VSDAVNAWREDGQQSIDGIFDQVESRFVAAWEDDAGLMTY GEAVADVLEAPEEWRAFAARASLHAARAKAKELGADPPWD CELAKTPEGYYQIRGGIPYAIAKSLAAAPFADILWMETKT ADLADARQFAEAIHAEFPDQMLAYNLSPSFNWDTTGMTDE EMRRFPEELGKMGFVFNFITYGGHQIDGVAAEEFATALRQ DGMLALARLQRKMRLVESPYRTPQTLVGGPRSDAALAASS GRTATTKALVQTEVPRKLLEEWLAMWSGHYQLKDKLRVQL RPQRAGSEVLELGIHGESDDKLANVIFQPIQDRRGRTILL VRDQNTFGAELRQKRLMTLIHLWLVHRFKAQAVHYVTPTD DNLYQTSKMKSHGIFTEVNQEVGEIIVAEVNHPRIAELLT PDRVALRKLITKE B:  HTPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQR GTIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPG QAVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLS QVPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDF RPFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRP GTKKQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVART DAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLAMVR RFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFGLVS DAVNAWREDGQQDGIFDQVESRFVAAWEDDAGLMTYGEAV ADVLEFGAPEEWRAFAARASLHAARAKAKELGADPPWDCE LAKTPEGYYQIRGGIPYAIAKSLAAAPFADILWMETKTAD LADARQFAEAIHAEFPDQMLAYNLSPSFNWDTTGMTDEEM RRFPEELGKMGFVFNFITYGGHQIDGVAAEEFATALRQDG MLALARLQRKMRLVESPYRTPQTLVGGPRSDAALAASSGR TATTKAMQTEVPRKLLEEWLAMWSGHYQLKDKLRVQLRPQ RAGSEVLELGIHGESDDKLANVIFQPIQDRRGRTILLVRD QNTFGAELRQKRLMTLIHLWLVHRFKAQAVHYVTPTDDNL YQTSKMKSHGIFTEVNQEVGEIIVAEVNHPRIAELLTPDR VALRKLITKE C:  HTPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQR GTIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPG QAVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLS QVPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDF RPFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRP GTKGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVARTDAE AANLIDSRADERDQPFLLGAVPSYKSCFLAMVRRFYELGV KELNGHLLYALGDSEYAAAGGWLERQGIFGLVSDAVNAWR EDGQQSIDGIFDQVESRFVAAWEDDAGLMTYGEAVADVMA PEEWRAFAARASLHAARAKAKELGADPPWDCELAKTPEGY YQIRGGIPYAIAKSLAAAPFADILWMETKTADLADARQFA EAIHAEFPDQMLAYNLSPSFNWDTTGMTDEEMRRFPEELG KMGFVFNFITYGGHQIDGVAAEEFATALRQDGMLALARLQ RKMRLVESPYRTPQTLVGGPRSDAALAASSGRTATTKAMG VQTEVPRKLLEEWLAMWSGHYQLKDKLRVQLRPQRAGSEV LELGIHGESDDKLANVIFQPIQDRRGRTILLVRDQNTFGA ELRQKRLMTLIHLWLVHRFKAQAVHYVTPTDDNLYQTSKM KSHGIFTEVNQEVGEIIVAEVNHPRIAELLTPDRVALRKL ITK D:  HTPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQR GTIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPG QAVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLS QVPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDF RPFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRP GTKKHQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVAR TDAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLAMV RRFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFGLV SDAVNAWREDGQQSIDGIFDQVESRFVAAWEDDAGLMTYG EAVADVLEAPEEWRAFAARASLHAARAKAKELGADPPWDC ELAKTPEGYYQIRGGIPYAIAKSLAAAPFADILWMETKTA DLADARQFAEAIHAEFPDQMLAYNLSPSFNWDTTGMTDEE MRRFPEELGKMGFVFNFITYGGHQIDGVAAEEFATALRQD GMLALARLQRKMRLVESPYRTPQTLVGGPRSDAALAASSG RTATTKAMGVQTEVPRKLLEEWLAMWSGHYQLKDKLRVQL RPQRAGSEVLELGIHGESDDKLANVIFQPIQDRRGRTILL VRDQNTFGAELRQKRLMTLIHLWLVHRFKAQAVHYVTPTD DNLYQTSKMKSHGIFTEVNQEVGEIIVAEVNHPRIAELLT PDRVALRKLITKE Description (1)  Isocitrate lyase 2 (E.C.4.1.3.1) Functional site 1) chain A residue 676 type sequence Q description binding site for residue ACO A 801 source : AC1 2) chain A residue 677 type sequence N description binding site for residue ACO A 801 source : AC1 3) chain A residue 678 type sequence T description binding site for residue ACO A 801 source : AC1 4) chain A residue 684 type sequence R description binding site for residue ACO A 801 source : AC1 5) chain A residue 685 type sequence Q description binding site for residue ACO A 801 source : AC1 6) chain A residue 686 type sequence K description binding site for residue ACO A 801 source : AC1 7) chain A residue 687 type sequence R description binding site for residue ACO A 801 source : AC1 8) chain A residue 689 type sequence M description binding site for residue ACO A 801 source : AC1 9) chain A residue 690 type sequence T description binding site for residue ACO A 801 source : AC1 10) chain A residue 708 type sequence V description binding site for residue ACO A 801 source : AC1 11) chain A residue 709 type sequence T description binding site for residue ACO A 801 source : AC1 12) chain A residue 710 type sequence P description binding site for residue ACO A 801 source : AC1 13) chain A residue 711 type sequence T description binding site for residue ACO A 801 source : AC1 14) chain A residue 713 type sequence D description binding site for residue ACO A 801 source : AC1 15) chain A residue 714 type sequence N description binding site for residue ACO A 801 source : AC1 16) chain A residue 716 type sequence Y description binding site for residue ACO A 801 source : AC1 17) chain A residue 717 type sequence Q description binding site for residue ACO A 801 source : AC1 18) chain A residue 720 type sequence K description binding site for residue ACO A 801 source : AC1 19) chain A residue 724 type sequence H description binding site for residue ACO A 801 source : AC1 20) chain A residue 764 type sequence K description binding site for residue ACO A 801 source : AC1 21) chain C residue 665 type sequence R description binding site for residue ACO A 801 source : AC1 22) chain B residue 673 type sequence V description binding site for residue ACO B 801 source : AC2 23) chain B residue 676 type sequence Q description binding site for residue ACO B 801 source : AC2 24) chain B residue 677 type sequence N description binding site for residue ACO B 801 source : AC2 25) chain B residue 678 type sequence T description binding site for residue ACO B 801 source : AC2 26) chain B residue 684 type sequence R description binding site for residue ACO B 801 source : AC2 27) chain B residue 685 type sequence Q description binding site for residue ACO B 801 source : AC2 28) chain B residue 686 type sequence K description binding site for residue ACO B 801 source : AC2 29) chain B residue 687 type sequence R description binding site for residue ACO B 801 source : AC2 30) chain B residue 689 type sequence M description binding site for residue ACO B 801 source : AC2 31) chain B residue 690 type sequence T description binding site for residue ACO B 801 source : AC2 32) chain B residue 708 type sequence V description binding site for residue ACO B 801 source : AC2 33) chain B residue 711 type sequence T description binding site for residue ACO B 801 source : AC2 34) chain B residue 713 type sequence D description binding site for residue ACO B 801 source : AC2 35) chain B residue 714 type sequence N description binding site for residue ACO B 801 source : AC2 36) chain B residue 716 type sequence Y description binding site for residue ACO B 801 source : AC2 37) chain B residue 717 type sequence Q description binding site for residue ACO B 801 source : AC2 38) chain B residue 720 type sequence K description binding site for residue ACO B 801 source : AC2 39) chain B residue 724 type sequence H description binding site for residue ACO B 801 source : AC2 40) chain B residue 764 type sequence K description binding site for residue ACO B 801 source : AC2 41) chain C residue 674 type sequence R description binding site for residue ACO C 801 source : AC3 42) chain C residue 675 type sequence D description binding site for residue ACO C 801 source : AC3 43) chain C residue 676 type sequence Q description binding site for residue ACO C 801 source : AC3 44) chain C residue 677 type sequence N description binding site for residue ACO C 801 source : AC3 45) chain C residue 678 type sequence T description binding site for residue ACO C 801 source : AC3 46) chain C residue 684 type sequence R description binding site for residue ACO C 801 source : AC3 47) chain C residue 685 type sequence Q description binding site for residue ACO C 801 source : AC3 48) chain C residue 686 type sequence K description binding site for residue ACO C 801 source : AC3 49) chain C residue 687 type sequence R description binding site for residue ACO C 801 source : AC3 50) chain C residue 689 type sequence M description binding site for residue ACO C 801 source : AC3 51) chain C residue 690 type sequence T description binding site for residue ACO C 801 source : AC3 52) chain C residue 708 type sequence V description binding site for residue ACO C 801 source : AC3 53) chain C residue 711 type sequence T description binding site for residue ACO C 801 source : AC3 54) chain C residue 713 type sequence D description binding site for residue ACO C 801 source : AC3 55) chain C residue 714 type sequence N description binding site for residue ACO C 801 source : AC3 56) chain C residue 716 type sequence Y description binding site for residue ACO C 801 source : AC3 57) chain C residue 717 type sequence Q description binding site for residue ACO C 801 source : AC3 58) chain C residue 720 type sequence K description binding site for residue ACO C 801 source : AC3 59) chain C residue 724 type sequence H description binding site for residue ACO C 801 source : AC3 60) chain D residue 716 type sequence Y description binding site for residue ACO C 801 source : AC3 61) chain B residue 665 type sequence R description binding site for residue ACO D 801 source : AC4 62) chain D residue 673 type sequence V description binding site for residue ACO D 801 source : AC4 63) chain D residue 676 type sequence Q description binding site for residue ACO D 801 source : AC4 64) chain D residue 677 type sequence N description binding site for residue ACO D 801 source : AC4 65) chain D residue 678 type sequence T description binding site for residue ACO D 801 source : AC4 66) chain D residue 684 type sequence R description binding site for residue ACO D 801 source : AC4 67) chain D residue 685 type sequence Q description binding site for residue ACO D 801 source : AC4 68) chain D residue 686 type sequence K description binding site for residue ACO D 801 source : AC4 69) chain D residue 687 type sequence R description binding site for residue ACO D 801 source : AC4 70) chain D residue 689 type sequence M description binding site for residue ACO D 801 source : AC4 71) chain D residue 690 type sequence T description binding site for residue ACO D 801 source : AC4 72) chain D residue 708 type sequence V description binding site for residue ACO D 801 source : AC4 73) chain D residue 709 type sequence T description binding site for residue ACO D 801 source : AC4 74) chain D residue 710 type sequence P description binding site for residue ACO D 801 source : AC4 75) chain D residue 711 type sequence T description binding site for residue ACO D 801 source : AC4 76) chain D residue 713 type sequence D description binding site for residue ACO D 801 source : AC4 77) chain D residue 714 type sequence N description binding site for residue ACO D 801 source : AC4 78) chain D residue 716 type sequence Y description binding site for residue ACO D 801 source : AC4 79) chain D residue 717 type sequence Q description binding site for residue ACO D 801 source : AC4 80) chain D residue 720 type sequence K description binding site for residue ACO D 801 source : AC4 81) chain D residue 724 type sequence H description binding site for residue ACO D 801 source : AC4 82) chain D residue 764 type sequence K description binding site for residue ACO D 801 source : AC4 83) chain A residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 84) chain B residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 85) chain B residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 86) chain B residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 87) chain C residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 88) chain C residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 89) chain C residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 90) chain C residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 91) chain C residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 92) chain D residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 93) chain A residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 94) chain D residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 95) chain D residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 96) chain D residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 97) chain D residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 98) chain A residue 216 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 99) chain A residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 100) chain A residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 101) chain A residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 102) chain B residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 103) chain B residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 104) chain A residue 215 type ACT_SITE sequence X description Proton acceptor => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI1 105) chain A residue 213-218 type prosite sequence KKXGHQ description ISOCITRATE_LYASE Isocitrate lyase signature. KKCGHQ source prosite : PS00161

Display surface Download Links