eF-site ID 6mso-D PDB Code 6mso Chain 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 D:  FNFVPLVSKVSHKETKYRLLTKDYVSVVQPGAGLPEMLRV DPAALTLLSSTAFDDVEHLLRSSHLMSLRKIFDDPEASDN DKFVALQLLKNANISSARLLPGCQDTGTAIIAGYRGDQVF VPGNDEEALSRGVYDIFQKRNFRYSQNVPLSMYDEKNTGT NLPAQIDLYASKGMEYSFMFVAKGGGSANKSFLLQETKSV LNPKSLRNFLKEKLAMFGTSACPPYHVAVVIGGTSAEMTM KVLKYASCHYYDDLITKPDMKTGYTFRDLELEEEVLKVCQ NIGMGAQFGGKYYAHDVRVIRMPRHGASCPIGIGVSCSAD RQALGKINKDGVWLEELEMEPSQYLPDLKTPAVMVNLNRP MPEVLQELSKHPVRTRLSLTGTIIVARDSAHARMREMLEA GKPLPQYMKEHPVYYAGPAKQPDGLPSGSFGPTTAGRMDP FVDLFQSHGGSMVMLAKGNRSKQVTKACHKYGGFYLGSIG GPAAVLAQNAIKKVECLDMKDLGMEAVWRIEVENFPAFIV VDDKGNDFFEQ Description Functional site 1) chain D residue 80 type sequence R description binding site for residue 1PE C 603 source : AE2 2) chain D residue 114 type sequence C description binding site for residue SF4 D 601 source : AE6 3) chain D residue 115 type sequence Q description binding site for residue SF4 D 601 source : AE6 4) chain D residue 232 type sequence A description binding site for residue SF4 D 601 source : AE6 5) chain D residue 233 type sequence C description binding site for residue SF4 D 601 source : AE6 6) chain D residue 328 type sequence C description binding site for residue SF4 D 601 source : AE6 7) chain D residue 330 type sequence A description binding site for residue SF4 D 601 source : AE6 8) chain D residue 474 type sequence K description binding site for residue SF4 D 601 source : AE6 9) chain D residue 115 type sequence Q description binding site for residue JYD D 602 source : AE7 10) chain D residue 116 type sequence D description binding site for residue JYD D 602 source : AE7 11) chain D residue 154 type sequence R description binding site for residue JYD D 602 source : AE7 12) chain D residue 197 type sequence G description binding site for residue JYD D 602 source : AE7 13) chain D residue 404 type sequence R description binding site for residue JYD D 602 source : AE7 14) chain D residue 450 type sequence T description binding site for residue JYD D 602 source : AE7 15) chain D residue 451 type sequence T description binding site for residue JYD D 602 source : AE7 16) chain D residue 454 type sequence R description binding site for residue JYD D 602 source : AE7 17) chain D residue 474 type sequence K description binding site for residue JYD D 602 source : AE7 18) chain D residue 33 type sequence K description binding site for residue 1PE D 603 source : AE8 19) chain D residue 341 type sequence D description binding site for residue 1PE D 603 source : AE8 20) chain D residue 114 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 21) chain D residue 233 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 22) chain D residue 328 type BINDING sequence C description BINDING => ECO:0000269|PubMed:30645090, ECO:0007744|PDB:6MSO source Swiss-Prot : SWS_FT_FI1 23) chain D residue 115 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 24) chain D residue 154 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 25) chain D residue 197 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 26) chain D residue 200 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 27) chain D residue 404 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 28) chain D residue 450 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2 29) chain D residue 474 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:E9AE57 source Swiss-Prot : SWS_FT_FI2

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