eF-site ID 6uoj-AB PDB Code 6uoj Chain A, B click to enlarge Title Crystal structure of cytosolic fumarate hydratase from Leishmania major in a complex with succinate Classification LYASE/LYASE INHIBITOR Compound Fumarate hydratase 2 Source (FUM2_LEIMA) Sequence A:  NADFHFSAIFQPTDPHHHQTEFAKVEGSEKYVEEVEVFGR QALKVNPEALTILAHRAFSDVHHFFRKDHLEGWRRAIEDP EASDNDRYVATTLLKNACIAAGRVLPSCQDTGTAIVLGKR GELCWTGGEDEKYLSKGIWNAYRYHNLRYSQTAALDMFKE CNTGDNLPAQLDLLAVPGSDYEFLFIAKGGGSANKAYLYQ ETKALLNPKSLRAFIEEKLKTLGTAACPPYHIALVIGGTS AEMTMKTVKLASCRYYDSLPTTGDKYGRAFRDPEWEKIVM EVAQKSGIGAQFGGKYFAHQARVIRLPRHGASCPVGLAVS CSADRQILAHINKSGIYIEQLEQNPAQYLPDTSVKVDLKR PIDKVRQQLSQYPVGTRVMLNGTLIVARDIAHAKIKEMMD NGEPLPEYMKTSPIYYAGPAKTPEGYASGSFGPTTAGRMD SYVDLFQSHGGSYITLAKGNRSKQVTDACKKHGGFYLGSI GGPAAILAKDSIKQVTCLAFPELGMEAVWKIEVEDFPAFI VVDDKGNDMYSKTLA B:  DFHFSAIFQPTDPHHHQTEFAKVEGSEKYVEEVEVFGRQA LKVNPEALTILAHRAFSDVHHFFRKDHLEGWRRAIEDPEA SDNDRYVATTLLKNACIAAGRVLPSCQDTGTAIVLGKRGE LCWTGGEDEKYLSKGIWNAYRYHNLRYSQTAALDMFKECN TGDNLPAQLDLLAVPGSDYEFLFIAKGGGSANKAYLYQET KALLNPKSLRAFIEEKLKTLGTAACPPYHIALVIGGTSAE MTMKTVKLASCRYYDSLPTTGDKYGRAFRDPEWEKIVMEV AQKSGIGAQFGGKYFAHQARVIRLPRHGASCPVGLAVSCS ADRQILAHINKSGIYIEQLEQNPAQYLPTSVKVDLKRPID KVRQQLSQYPVGTRVMLNGTLIVARDIAHAKIKEMMDNGE PLPEYMKTSPIYYAGPAKTPEGYASGSFGPTTAGRMDSYV DLFQSHGGSYITLAKGNRSKQVTDACKKHGGFYLGSIGGP AAILAKDSIKQVTCLAFPELGMEAVWKIEVEDFPAFIVVD DKGNDMYSKTLA Description Functional site 1) chain A residue 133 type sequence C description binding site for residue SF4 A 601 source : AC1 2) chain A residue 135 type sequence D description binding site for residue SF4 A 601 source : AC1 3) chain A residue 214 type sequence G description binding site for residue SF4 A 601 source : AC1 4) chain A residue 251 type sequence A description binding site for residue SF4 A 601 source : AC1 5) chain A residue 252 type sequence C description binding site for residue SF4 A 601 source : AC1 6) chain A residue 346 type sequence C description binding site for residue SF4 A 601 source : AC1 7) chain A residue 348 type sequence A description binding site for residue SF4 A 601 source : AC1 8) chain A residue 134 type sequence Q description binding site for residue SIN A 602 source : AC2 9) chain A residue 135 type sequence D description binding site for residue SIN A 602 source : AC2 10) chain A residue 173 type sequence R description binding site for residue SIN A 602 source : AC2 11) chain A residue 216 type sequence G description binding site for residue SIN A 602 source : AC2 12) chain A residue 421 type sequence R description binding site for residue SIN A 602 source : AC2 13) chain A residue 467 type sequence T description binding site for residue SIN A 602 source : AC2 14) chain A residue 468 type sequence T description binding site for residue SIN A 602 source : AC2 15) chain A residue 471 type sequence R description binding site for residue SIN A 602 source : AC2 16) chain A residue 491 type sequence K description binding site for residue SIN A 602 source : AC2 17) chain B residue 336 type sequence A description binding site for residue SIN A 602 source : AC2 18) chain B residue 133 type sequence C description binding site for residue SF4 B 601 source : AC3 19) chain B residue 134 type sequence Q description binding site for residue SF4 B 601 source : AC3 20) chain B residue 214 type sequence G description binding site for residue SF4 B 601 source : AC3 21) chain B residue 252 type sequence C description binding site for residue SF4 B 601 source : AC3 22) chain B residue 346 type sequence C description binding site for residue SF4 B 601 source : AC3 23) chain B residue 348 type sequence A description binding site for residue SF4 B 601 source : AC3 24) chain B residue 491 type sequence K description binding site for residue SF4 B 601 source : AC3 25) chain A residue 334 type sequence H description binding site for residue SIN B 602 source : AC4 26) chain B residue 134 type sequence Q description binding site for residue SIN B 602 source : AC4 27) chain B residue 135 type sequence D description binding site for residue SIN B 602 source : AC4 28) chain B residue 173 type sequence R description binding site for residue SIN B 602 source : AC4 29) chain B residue 216 type sequence G description binding site for residue SIN B 602 source : AC4 30) chain B residue 421 type sequence R description binding site for residue SIN B 602 source : AC4 31) chain B residue 467 type sequence T description binding site for residue SIN B 602 source : AC4 32) chain B residue 468 type sequence T description binding site for residue SIN B 602 source : AC4 33) chain B residue 471 type sequence R description binding site for residue SIN B 602 source : AC4 34) chain B residue 491 type sequence K description binding site for residue SIN B 602 source : AC4 35) chain B residue 55 type sequence K description binding site for residue GOL B 603 source : AC5 36) chain B residue 71 type sequence N description binding site for residue GOL B 603 source : AC5 37) chain A residue 65 type sequence R description binding site for residue GOL B 604 source : AC6 38) chain B residue 70 type sequence V description binding site for residue GOL B 604 source : AC6 39) chain B residue 72 type sequence P description binding site for residue GOL B 604 source : AC6 40) chain B residue 150 type sequence W description binding site for residue GOL B 604 source : AC6 41) chain B residue 151 type sequence T description binding site for residue GOL B 604 source : AC6 42) chain A residue 133 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 43) chain A residue 491 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 44) chain B residue 133 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 45) chain B residue 134 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 46) chain B residue 173 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 47) chain B residue 216 type BINDING sequence G description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 48) chain B residue 219 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 49) chain B residue 252 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 50) chain B residue 346 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 51) chain B residue 421 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 52) chain B residue 467 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 53) chain A residue 134 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 54) chain B residue 491 type BINDING sequence K description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 55) chain A residue 173 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 56) chain A residue 216 type BINDING sequence G description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 57) chain A residue 219 type BINDING sequence N description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 58) chain A residue 252 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 59) chain A residue 346 type BINDING sequence C description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 60) chain A residue 421 type BINDING sequence R description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1 61) chain A residue 467 type BINDING sequence T description BINDING => ECO:0000269|PubMed:27528683, ECO:0007744|PDB:5L2R source Swiss-Prot : SWS_FT_FI1

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