eF-site ID 6edw-B PDB Code 6edw Chain B click to enlarge Title Crystal structure of Mycobacterium tuberculosis ICL2 in the apo form Classification LYASE Compound Isocitrate lyase 2 Source (ACEA2_MYCTO) Sequence B:  TPFEQDFEKDVAATQRYFDSSRFAGIIRLYTARQVVEQRG TIPVDHIVAREAAGAFYERLRELFAARKSITTFGPYSPGQ AVSMKRMGIEAIYLGGWATSAKGSSTEDPGPDLASYPLSQ VPDDAAVLVRALLTADRNQHYLRLQMSERQRAATPAYDFR PFIIADADTGHGGDPHVRNLIRRFVEVGVPGYHIEDQRPG TKKXGHQGGKVLVPSDEQIKRLNAARFQLDIMRVPGIIVA RTDAEAANLIDSRADERDQPFLLGATKLDVPSYKSCFLAM VRRFYELGVKELNGHLLYALGDSEYAAAGGWLERQGIFGL VSDAVNAWREDGQQSIDGIFDQVESRFVAAWEDDAGLMTY GEAVADVLEFGQSEGEPIGMAPEEWRAFAARASLHAARAK AKELGADPPWDCELAKTPEGYYQIRGGIPYAIAKSLAAAP FADILWMETKTADLADARQFAEAIHAEFPDQMLAYNLSPS FNWDTTGMTDEEMRRFPEELGKMGFVFNFITYGGHQIDGV AAEEFATALRQDGMLALARLQRKMRLVESPYRTPQTLVGG PRSDAALAASSGRTATTKAMGHLVQTEVPRKLLEEWLAMW SGHYQLKDKLRVQLRPQRAGSEVLELGIHGESDDKLANVI FQPIQDRRGRTILLVRDQNTFGAELRQKRLMTLIHLWLVH RFKAQAVHYVTPTDDNLYQTSKMKSHGIFTEVNQEVGEII VAEVNHPRIAELLTPDRVALRKLITK Description (1)  Isocitrate lyase 2 (E.C.4.1.3.1) Functional site 1) chain B residue 151 type sequence H description binding site for residue GOL A 801 source : AC1 2) chain B residue 18 type sequence F description binding site for residue GOL A 802 source : AC2 3) chain B residue 51 type sequence G description binding site for residue GOL A 802 source : AC2 4) chain B residue 52 type sequence T description binding site for residue GOL A 802 source : AC2 5) chain B residue 450 type sequence A description binding site for residue MG B 801 source : AC5 6) chain B residue 453 type sequence A description binding site for residue MG B 801 source : AC5 7) chain B residue 482 type sequence Q description binding site for residue MG B 801 source : AC5 8) chain B residue 252 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 487 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 10) chain B residue 522 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 106 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 12) chain B residue 177 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 216 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 215 type ACT_SITE sequence X description Proton acceptor => ECO:0000250|UniProtKB:P9WKK7 source Swiss-Prot : SWS_FT_FI1

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