eF-site ID 6mso-ABCD PDB Code 6mso Chain A, B, C, D click to enlarge Title Crystal structure of mitochondrial fumarate hydratase from Leishmania major in a complex with inhibitor thiomalate Classification LYASE/LYASE inhibitor Compound fumarate hydratase Source (Q4QAU9_LEIMA) Sequence A:  AEFNFVPLVSKVSHKETKYRLLTKDYVSVVQPGAGLPEML RVDPAALTLLSSTAFDDVEHLLRSSHLMSLRKIFDDPEAS DNDKFVALQLLKNANISSARLLPGCQDTGTAIIAGYRGDQ VFVPGNDEEALSRGVYDIFQKRNFRYSQNVPLSMYDEKNT GTNLPAQIDLYASKGMEYSFMFVAKGGGSANKSFLLQETK SVLNPKSLRNFLKEKLAMFGTSACPPYHVAVVIGGTSAEM TMKVLKYASCHYYDDLITKPDMKTGYTFRDLELEEEVLKV CQNIGMGAQFGGKYYAHDVRVIRMPRHGASCPIGIGVSCS ADRQALGKINKDGVWLEELEMEPSQYLPDLKEDELLKTPA VMVNLNRPMPEVLQELSKHPVRTRLSLTGTIIVARDSAHA RMREMLEAGKPLPQYMKEHPVYYAGPAKQPDGLPSGSFGP TTAGRMDPFVDLFQSHGGSMVMLAKGNRSKQVTKACHKYG GFYLGSIGGPAAVLAQNAIKKVECLDMKDLGMEAVWRIEV ENFPAFIVVDDKGNDFFEQL B:  AEFNFVPLVSKVSHKETKYRLLTKDYVSVVQPGAGLPEML RVDPAALTLLSSTAFDDVEHLLRSSHLMSLRKIFDDPEAS DNDKFVALQLLKNANISSARLLPGCQDTGTAIIAGYRGDQ VFVPGNDEEALSRGVYDIFQKRNFRYSQNVPLSMYDEKNT GTNLPAQIDLYASKGMEYSFMFVAKGGGSANKSFLLQETK SVLNPKSLRNFLKEKLAMFGTSACPPYHVAVVIGGTSAEM TMKVLKYASCHYYDDLITKPDMKTGYTFRDLELEEEVLKV CQNIGMGAQFGGKYYAHDVRVIRMPRHGASCPIGIGVSCS ADRQALGKINKDGVWLEELEMEPSQYLPDLKEDELLKTPA VMVNLNRPMPEVLQELSKHPVRTRLSLTGTIIVARDSAHA RMREMLEAGKPLPQYMKEHPVYYAGPAKQPDGLPSGSFGP TTAGRMDPFVDLFQSHGGSMVMLAKGNRSKQVTKACHKYG GFYLGSIGGPAAVLAQNAIKKVECLDMKDLGMEAVWRIEV ENFPAFIVVDDKGNDFFEQL C:  FNFVPLVSKVSHKETKYRLLTKDYVSVVQPGAGLPEMLRV DPAALTLLSSTAFDDVEHLLRSSHLMSLRKIFDDPEASDN DKFVALQLLKNANISSARLLPGCQDTGTAIIAGYRGDQVF VPGNDEEALSRGVYDIFQKRNFRYSQNVPLSMYDEKNTGT NLPAQIDLYASKGMEYSFMFVAKGGGSANKSFLLQETKSV LNPKSLRNFLKEKLAMFGTSACPPYHVAVVIGGTSAEMTM KVLKYASCHYYDDLITKPDMKTGYTFRDLELEEEVLKVCQ NIGMGAQFGGKYYAHDVRVIRMPRHGASCPIGIGVSCSAD RQALGKINKDGVWLEELEMEPSQYLPTPAVMVNLNRPMPE VLQELSKHPVRTRLSLTGTIIVARDSAHARMREMLEAGKP LPQYMKEHPVYYAGPAKQPDGLPSGSFGPTTAGRMDPFVD LFQSHGGSMVMLAKGNRSKQVTKACHKYGGFYLGSIGGPA AVLAQNAIKKVECLDMKDLGMEAVWRIEVENFPAFIVVDD KGNDFFEQ D:  FNFVPLVSKVSHKETKYRLLTKDYVSVVQPGAGLPEMLRV DPAALTLLSSTAFDDVEHLLRSSHLMSLRKIFDDPEASDN DKFVALQLLKNANISSARLLPGCQDTGTAIIAGYRGDQVF VPGNDEEALSRGVYDIFQKRNFRYSQNVPLSMYDEKNTGT NLPAQIDLYASKGMEYSFMFVAKGGGSANKSFLLQETKSV LNPKSLRNFLKEKLAMFGTSACPPYHVAVVIGGTSAEMTM KVLKYASCHYYDDLITKPDMKTGYTFRDLELEEEVLKVCQ NIGMGAQFGGKYYAHDVRVIRMPRHGASCPIGIGVSCSAD RQALGKINKDGVWLEELEMEPSQYLPDLKTPAVMVNLNRP MPEVLQELSKHPVRTRLSLTGTIIVARDSAHARMREMLEA GKPLPQYMKEHPVYYAGPAKQPDGLPSGSFGPTTAGRMDP FVDLFQSHGGSMVMLAKGNRSKQVTKACHKYGGFYLGSIG GPAAVLAQNAIKKVECLDMKDLGMEAVWRIEVENFPAFIV VDDKGNDFFEQ Description Functional site 1) chain A residue 114 type sequence C description binding site for residue SF4 A 601 source : AC1 2) chain A residue 115 type sequence Q description binding site for residue SF4 A 601 source : AC1 3) chain A residue 195 type sequence G description binding site for residue SF4 A 601 source : AC1 4) chain A residue 233 type sequence C description binding site for residue SF4 A 601 source : AC1 5) chain A residue 328 type sequence C description binding site for residue SF4 A 601 source : AC1 6) chain A residue 330 type sequence A description binding site for residue SF4 A 601 source : AC1 7) chain A residue 474 type sequence K description binding site for residue SF4 A 601 source : AC1 8) chain A residue 23 type sequence H description binding site for residue GOL A 602 source : AC2 9) chain A residue 28 type sequence Y description binding site for residue GOL A 602 source : AC2 10) chain A residue 337 type sequence K description binding site for residue GOL A 602 source : AC2 11) chain A residue 288 type sequence K description binding site for residue GOL A 603 source : AC3 12) chain A residue 291 type sequence Q description binding site for residue GOL A 603 source : AC3 13) chain A residue 302 type sequence K description binding site for residue GOL A 603 source : AC3 14) chain A residue 150 type sequence K description binding site for residue GOL A 604 source : AC4 15) chain A residue 151 type sequence R description binding site for residue GOL A 604 source : AC4 16) chain A residue 278 type sequence R description binding site for residue GOL A 605 source : AC5 17) chain A residue 307 type sequence D description binding site for residue GOL A 605 source : AC5 18) chain A residue 309 type sequence R description binding site for residue GOL A 605 source : AC5 19) chain A residue 438 type sequence Q description binding site for residue GOL A 606 source : AC6 20) chain A residue 30 type sequence L description binding site for residue 1PE A 607 source : AC7 21) chain A residue 33 type sequence K description binding site for residue 1PE A 607 source : AC7 22) chain A residue 341 type sequence D description binding site for residue 1PE A 607 source : AC7 23) chain A residue 344 type sequence W description binding site for residue 1PE A 607 source : AC7 24) chain A residue 115 type sequence Q description binding site for residue JYD A 608 source : AC8 25) chain A residue 116 type sequence D description binding site for residue JYD A 608 source : AC8 26) chain A residue 154 type sequence R description binding site for residue JYD A 608 source : AC8 27) chain A residue 196 type sequence G description binding site for residue JYD A 608 source : AC8 28) chain A residue 197 type sequence G description binding site for residue JYD A 608 source : AC8 29) chain A residue 404 type sequence R description binding site for residue JYD A 608 source : AC8 30) chain A residue 450 type sequence T description binding site for residue JYD A 608 source : AC8 31) chain A residue 451 type sequence T description binding site for residue JYD A 608 source : AC8 32) chain A residue 454 type sequence R description binding site for residue JYD A 608 source : AC8 33) chain A residue 474 type sequence K description binding site for residue JYD A 608 source : AC8 34) chain A residue 354 type sequence Q description binding site for residue 1PE A 609 source : AC9 35) chain B residue 354 type sequence Q description binding site for residue 1PE A 609 source : AC9 36) chain B residue 355 type sequence Y description binding site for residue 1PE A 609 source : AC9 37) chain A residue 409 type sequence A description binding site for residue 1PE A 610 source : AD1 38) chain A residue 412 type sequence R description binding site for residue 1PE A 610 source : AD1 39) chain A residue 413 type sequence E description binding site for residue 1PE A 610 source : AD1 40) chain A residue 416 type sequence E description binding site for residue 1PE A 610 source : AD1 41) chain B residue 213 type sequence N description binding site for residue 1PE A 610 source : AD1 42) chain B residue 216 type sequence S description binding site for residue 1PE A 610 source : AD1 43) chain A residue 463 type sequence Q description binding site for residue 1PE A 611 source : AD2 44) chain A residue 466 type sequence G description binding site for residue 1PE A 611 source : AD2 45) chain A residue 488 type sequence Y description binding site for residue 1PE A 611 source : AD2 46) chain B residue 114 type sequence C description binding site for residue SF4 B 601 source : AD3 47) chain B residue 115 type sequence Q description binding site for residue SF4 B 601 source : AD3 48) chain B residue 195 type sequence G description binding site for residue SF4 B 601 source : AD3 49) chain B residue 233 type sequence C description binding site for residue SF4 B 601 source : AD3 50) chain B residue 328 type sequence C description binding site for residue SF4 B 601 source : AD3 51) chain B residue 330 type sequence A description binding site for residue SF4 B 601 source : AD3 52) chain B residue 474 type sequence K description binding site for residue SF4 B 601 source : AD3 53) chain B residue 23 type sequence H description binding site for residue GOL B 602 source : AD4 54) chain B residue 28 type sequence Y description binding site for residue GOL B 602 source : AD4 55) chain B residue 337 type sequence K description binding site for residue GOL B 602 source : AD4 56) chain B residue 520 type sequence G description binding site for residue GOL B 603 source : AD5 57) chain B residue 521 type sequence M description binding site for residue GOL B 603 source : AD5 58) chain B residue 115 type sequence Q description binding site for residue JYD B 604 source : AD6 59) chain B residue 116 type sequence D description binding site for residue JYD B 604 source : AD6 60) chain B residue 154 type sequence R description binding site for residue JYD B 604 source : AD6 61) chain B residue 196 type sequence G description binding site for residue JYD B 604 source : AD6 62) chain B residue 197 type sequence G description binding site for residue JYD B 604 source : AD6 63) chain B residue 404 type sequence R description binding site for residue JYD B 604 source : AD6 64) chain B residue 450 type sequence T description binding site for residue JYD B 604 source : AD6 65) chain B residue 451 type sequence T description binding site for residue JYD B 604 source : AD6 66) chain B residue 454 type sequence R description binding site for residue JYD B 604 source : AD6 67) chain B residue 474 type sequence K description binding site for residue JYD B 604 source : AD6 68) chain B residue 33 type sequence K description binding site for residue 1PE B 605 source : AD7 69) chain B residue 341 type sequence D description binding site for residue 1PE B 605 source : AD7 70) chain B residue 87 type sequence E description binding site for residue 1PE B 606 source : AD8 71) chain B residue 291 type sequence Q description binding site for residue 1PE B 606 source : AD8 72) chain B residue 302 type sequence K description binding site for residue 1PE B 606 source : AD8 73) chain C residue 114 type sequence C description binding site for residue SF4 C 601 source : AD9 74) chain C residue 115 type sequence Q description binding site for residue SF4 C 601 source : AD9 75) chain C residue 195 type sequence G description binding site for residue SF4 C 601 source : AD9 76) chain C residue 232 type sequence A description binding site for residue SF4 C 601 source : AD9 77) chain C residue 233 type sequence C description binding site for residue SF4 C 601 source : AD9 78) chain C residue 328 type sequence C description binding site for residue SF4 C 601 source : AD9 79) chain C residue 330 type sequence A description binding site for residue SF4 C 601 source : AD9 80) chain C residue 474 type sequence K description binding site for residue SF4 C 601 source : AD9 81) chain C residue 215 type sequence K description binding site for residue GOL C 602 source : AE1 82) chain C residue 216 type sequence S description binding site for residue GOL C 602 source : AE1 83) chain C residue 219 type sequence N description binding site for residue GOL C 602 source : AE1 84) chain C residue 354 type sequence Q description binding site for residue 1PE C 603 source : AE2 85) chain D residue 80 type sequence R description binding site for residue 1PE C 603 source : AE2 86) chain C residue 115 type sequence Q description binding site for residue JYD C 604 source : AE3 87) chain C residue 116 type sequence D description binding site for residue JYD C 604 source : AE3 88) chain C residue 154 type sequence R description binding site for residue JYD C 604 source : AE3 89) chain C residue 196 type sequence G description binding site for residue JYD C 604 source : AE3 90) chain C residue 197 type sequence G description binding site for residue JYD C 604 source : AE3 91) chain C residue 404 type sequence R description binding site for residue JYD C 604 source : AE3 92) chain C residue 450 type sequence T description binding site for residue JYD C 604 source : AE3 93) chain C residue 451 type sequence T description binding site for residue JYD C 604 source : AE3 94) chain C residue 454 type sequence R description binding site for residue JYD C 604 source : AE3 95) chain C residue 474 type sequence K description binding site for residue JYD C 604 source : AE3 96) chain C residue 87 type sequence E description binding site for residue 1PE C 605 source : AE4 97) chain C residue 284 type sequence E description binding site for residue 1PE C 605 source : AE4 98) chain C residue 288 type sequence K description binding site for residue 1PE C 605 source : AE4 99) chain C residue 291 type sequence Q description binding site for residue 1PE C 605 source : AE4 100) chain C residue 302 type sequence K description binding site for residue 1PE C 605 source : AE4 101) chain C residue 78 type sequence S description binding site for residue 1PE C 606 source : AE5 102) chain C residue 81 type sequence K description binding site for residue 1PE C 606 source : AE5 103) chain C residue 303 type sequence Y description binding site for residue 1PE C 606 source : AE5 104) chain C residue 306 type sequence H description binding site for residue 1PE C 606 source : AE5 105) chain C residue 307 type sequence D description binding site for residue 1PE C 606 source : AE5 106) chain C residue 309 type sequence R description binding site for residue 1PE C 606 source : AE5 107) chain D residue 114 type sequence C description binding site for residue SF4 D 601 source : AE6 108) chain D residue 115 type sequence Q description binding site for residue SF4 D 601 source : AE6 109) chain D residue 232 type sequence A description binding site for residue SF4 D 601 source : AE6 110) chain D residue 233 type sequence C description binding site for residue SF4 D 601 source : AE6 111) chain D residue 328 type sequence C description binding site for residue SF4 D 601 source : AE6 112) chain D residue 330 type sequence A description binding site for residue SF4 D 601 source : AE6 113) chain D residue 474 type sequence K description binding site for residue SF4 D 601 source : AE6 114) chain D residue 115 type sequence Q description binding site for residue JYD D 602 source : AE7 115) chain D residue 116 type sequence D description binding site for residue JYD D 602 source : AE7 116) chain D residue 154 type sequence R description binding site for residue JYD D 602 source : AE7 117) chain D residue 197 type sequence G description binding site for residue JYD D 602 source : AE7 118) chain D residue 404 type sequence R description binding site for residue JYD D 602 source : AE7 119) chain D residue 450 type sequence T description binding site for residue JYD D 602 source : AE7 120) chain D residue 451 type sequence T description binding site for residue JYD D 602 source : AE7 121) chain D residue 454 type sequence R description binding site for residue JYD D 602 source : AE7 122) chain D residue 474 type sequence K description binding site for residue JYD D 602 source : AE7 123) chain B residue 487 type sequence K description binding site for residue 1PE D 603 source : AE8 124) chain B residue 488 type sequence Y description binding site for residue 1PE D 603 source : AE8 125) chain D residue 33 type sequence K description binding site for residue 1PE D 603 source : AE8 126) chain D residue 341 type sequence D description binding site for residue 1PE D 603 source : AE8 127) chain A residue 467-476 type prosite sequence GSMVMLAKGN description FUMARATE_LYASES Fumarate lyases signature. GSmvMlAKgN source prosite : PS00163 128) chain A residue 114 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 129) chain D residue 114 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 130) chain D residue 233 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 131) chain D residue 328 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 132) chain A residue 233 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 133) chain A residue 328 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 134) chain B residue 114 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 135) chain B residue 233 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 136) chain B residue 328 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 137) chain C residue 114 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 138) chain C residue 233 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 139) chain C residue 328 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 140) chain A residue 115 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 141) chain B residue 197 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 142) chain B residue 200 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 143) chain B residue 404 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 144) chain B residue 450 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 145) chain B residue 474 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 146) chain C residue 115 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 147) chain C residue 154 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 148) chain C residue 197 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 149) chain C residue 200 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 150) chain C residue 404 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 151) chain A residue 154 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 152) chain C residue 450 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 153) chain C residue 474 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 154) chain D residue 115 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 155) chain D residue 154 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 156) chain D residue 197 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 157) chain D residue 200 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 158) chain D residue 404 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 159) chain D residue 450 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 160) chain D residue 474 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 161) chain A residue 197 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 162) chain A residue 200 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 163) chain A residue 404 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 164) chain A residue 450 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 165) chain A residue 474 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 166) chain B residue 115 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 167) chain B residue 154 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2

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