eF-site ID 5h8u-AB PDB Code 5h8u Chain A, B click to enlarge Title Crystal structure of mycobacterium tuberculosis wild-type malate synthase in complex with product malate Classification TRANSFERASE Compound Malate synthase G Source Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (MASZ_MYCTU) Sequence A:  DRVSVGNLRIARVLYDFVNNEALPGTDIDPDSFWAGVDKV VADLTPQNQALLNARDELQAQIDKWHRRRVIEPIDMDAYR QFLTEIGYLLPEPDDFTITTSGVDAEITTTAGPQLVVPVL NARFALNAANARWGSLYDALYGTDVIPETDGAEKGPTYNK VRGDKVIAYARKFLDDSVPLSSGSFGDATGFTVQDGQLVV ALPDKSTGLANPGQFAGYTGAAESPTSVLLINHGLHIEIL IDPESQVGTTDRAGVKDVILESAITTIMDFEDSVAAVDAA DKVLGYRNWLGLNKGDLAAAVAFLRVLNRDRNYTAPGGGQ FTLPGRSLMFVRNVGHLMTNDAIVDTDGSEVFEGIMDALF TGLIAIHGLKASDVNGPLINSRTGSIYIVKPKMHGPAEVA FTCELFSRVEDVLGLPQNTMKIGIMDEERRTTVNLKACIK AAADRVVFINTGFLDRTGDEIHTSMEAGPMVRKGTMKSQP WILAYEDHNVDAGLAAGFSGRAQVGKGMWTMTELMADMVE TKIAQPRAGASTAWVPSPTAATLHALHYHQVDVAAVQQGL AGKRRATIEQLLTIPLAKELAWAPDEIREEVDNNCQSILG YVVRWVDQGVGCSKVPDIHDVALMEDRATLRISSQLLANW LRHGVITSADVRASLERMAPLVDRQNAGDVAYRPMAPNFD DSIAFLAAQELILSGAQQPNGYTEPILHRRRREFKARAAE B:  DRVSVGNLRIARVLYDFVNNEALPGTDIDPDSFWAGVDKV VADLTPQNQALLNARDELQAQIDKWHRRRVIEPIDMDAYR QFLTEIGYLLPEPDDFTITTSGVDAEITTTAGPQLVVPVL NARFALNAANARWGSLYDALYGTDVIPETEKGPTYNKVRG DKVIAYARKFLDDSVPLSSGSFGDATGFTVQDGQLVVALP DKSTGLANPGQFAGYTGAAESPTSVLLINHGLHIEILIDP ESQVGTTDRAGVKDVILESAITTIMDFEDSVAAVDAADKV LGYRNWLGLNKGDLAAAVFLRVLNRDRNYTAPGGGQFTLP GRSLMFVRNVGHLMTNDAIVDTDGSEVFEGIMDALFTGLI AIHGLKASDVNGPLINSRTGSIYIVKPKMHGPAEVAFTCE LFSRVEDVLGLPQNTMKIGIMDEERRTTVNLKACIKAAAD RVVFINTGFLDRTGDEIHTSMEAGPMVRKGTMKSQPWILA YEDHNVDAGLAAGFSGRAQVGKGMWTMTELMADMVETKIA QPRAGASTAWVPSPTAATLHALHYHQVDVAAVQQGLAGKR RATIEQLLTIPLAKELAWAPDEIREEVDNNCQSILGYVVR WVDQGVGCSKVPDIHDVALMEDRATLRISSQLLANWLRHG VITSADVRASLERMAPLVDRQNAGDVAYRPMAPNFDDSIA FLAAQELILSGAQQPNGYTEPILHRRRREFKARAAE Description Functional site 1) chain A residue 434 type sequence E description binding site for residue MG A 801 source : AC1 2) chain A residue 462 type sequence D description binding site for residue MG A 801 source : AC1 3) chain A residue 274 type sequence D description binding site for residue LMR A 802 source : AC2 4) chain A residue 339 type sequence R description binding site for residue LMR A 802 source : AC2 5) chain A residue 434 type sequence E description binding site for residue LMR A 802 source : AC2 6) chain A residue 459 type sequence G description binding site for residue LMR A 802 source : AC2 7) chain A residue 460 type sequence F description binding site for residue LMR A 802 source : AC2 8) chain A residue 461 type sequence L description binding site for residue LMR A 802 source : AC2 9) chain A residue 462 type sequence D description binding site for residue LMR A 802 source : AC2 10) chain A residue 541 type sequence W description binding site for residue LMR A 802 source : AC2 11) chain A residue 633 type sequence D description binding site for residue LMR A 802 source : AC2 12) chain A residue 635 type sequence A description binding site for residue LMR A 802 source : AC2 13) chain B residue 434 type sequence E description binding site for residue MG B 801 source : AC3 14) chain B residue 462 type sequence D description binding site for residue MG B 801 source : AC3 15) chain A residue 557 type sequence Q description binding site for residue MG B 802 source : AC4 16) chain B residue 69 type sequence R description binding site for residue MG B 802 source : AC4 17) chain B residue 274 type sequence D description binding site for residue GLV B 803 source : AC5 18) chain B residue 339 type sequence R description binding site for residue GLV B 803 source : AC5 19) chain B residue 434 type sequence E description binding site for residue GLV B 803 source : AC5 20) chain B residue 459 type sequence G description binding site for residue GLV B 803 source : AC5 21) chain B residue 460 type sequence F description binding site for residue GLV B 803 source : AC5 22) chain B residue 461 type sequence L description binding site for residue GLV B 803 source : AC5 23) chain B residue 462 type sequence D description binding site for residue GLV B 803 source : AC5 24) chain B residue 541 type sequence W description binding site for residue GLV B 803 source : AC5 25) chain A residue 118 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 26) chain A residue 543 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 27) chain A residue 618 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 28) chain A residue 633 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 29) chain B residue 118 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 30) chain B residue 125 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 31) chain B residue 275 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 32) chain B residue 312 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 33) chain B residue 339 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 34) chain B residue 434 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 35) chain A residue 125 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 36) chain B residue 459 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 37) chain B residue 462 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 38) chain B residue 543 type BINDING sequence P description source Swiss-Prot : SWS_FT_FI3 39) chain B residue 618 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 40) chain B residue 633 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 41) chain A residue 275 type BINDING sequence S description source Swiss-Prot : SWS_FT_FI3 42) chain A residue 312 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 43) chain A residue 339 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 44) chain A residue 434 type BINDING sequence E description source Swiss-Prot : SWS_FT_FI3 45) chain A residue 459 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 46) chain A residue 462 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 47) chain A residue 619 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00641 source Swiss-Prot : SWS_FT_FI4 48) chain B residue 619 type MOD_RES sequence C description Cysteine sulfenic acid (-SOH) => ECO:0000255|HAMAP-Rule:MF_00641 source Swiss-Prot : SWS_FT_FI4 49) chain A residue 339 type ACT_SITE sequence R description Proton acceptor source Swiss-Prot : SWS_FT_FI1 50) chain B residue 339 type ACT_SITE sequence R description Proton acceptor source Swiss-Prot : SWS_FT_FI1 51) chain A residue 633 type ACT_SITE sequence D description Proton donor source Swiss-Prot : SWS_FT_FI2 52) chain B residue 633 type ACT_SITE sequence D description Proton donor source Swiss-Prot : SWS_FT_FI2

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