eF-site ID 1pkn-A PDB Code 1pkn Chain A click to enlarge Title STRUCTURE OF RABBIT MUSCLE PYRUVATE KINASE COMPLEXED WITH MN2+, K+, AND PYRUVATE Classification PHOSPHOTRANSFERASE Compound PYRUVATE KINASE Source Oryctolagus cuniculus (Rabbit) (KPYM_RABIT) Sequence A:  IQTQQLHAAMADTFLEHMCRLDIDSAPITARNTGIICTIG PASRSVETLKEMIKSGMNVARMNFSHGTHEYHAETIKNVR TATESFASDPILYRPVAVALDTKGPEIRTGLIKGSELKKG ATLKITLDNAYMAACDENILWLDYKNICKVVEVGSKVYVD DGLISLQVKQKGPDFLVTEVENGGFLGSKKGVNLPGAAVD LPAVSEKDIQDLKFGVDEDVDMVFASFIRKAADVHEVRKI LGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDL GIEIPAEKVFLAQKMIIGRCNRAGKPVICATQMLESMIKK PRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRM QHLIAREAEAAMFHRKLFEELARSSSHSTDLMEAMAMGSV EASYKCLAAALIVLTESGRSAHQVARYRPRAPIIAVTRNH QTARQAHLYRGIFPVVCKDPVQEAWAEDVDLRVNLAMNVG KAAGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP Description Functional site 1) chain A residue 74 type sequence N description BINDING SITE FOR RESIDUE K A 532 source : AC1 2) chain A residue 76 type sequence S description BINDING SITE FOR RESIDUE K A 532 source : AC1 3) chain A residue 112 type sequence D description BINDING SITE FOR RESIDUE K A 532 source : AC1 4) chain A residue 113 type sequence T description BINDING SITE FOR RESIDUE K A 532 source : AC1 5) chain A residue 271 type sequence E description BINDING SITE FOR RESIDUE MN A 534 source : AC2 6) chain A residue 295 type sequence D description BINDING SITE FOR RESIDUE MN A 534 source : AC2 7) chain A residue 269 type sequence K description BINDING SITE FOR RESIDUE PYR A 533 source : AC3 8) chain A residue 271 type sequence E description BINDING SITE FOR RESIDUE PYR A 533 source : AC3 9) chain A residue 290 type sequence M description BINDING SITE FOR RESIDUE PYR A 533 source : AC3 10) chain A residue 292 type sequence A description BINDING SITE FOR RESIDUE PYR A 533 source : AC3 11) chain A residue 294 type sequence G description BINDING SITE FOR RESIDUE PYR A 533 source : AC3 12) chain A residue 295 type sequence D description BINDING SITE FOR RESIDUE PYR A 533 source : AC3 13) chain A residue 327 type sequence T description BINDING SITE FOR RESIDUE PYR A 533 source : AC3 14) chain A residue 73 type catalytic sequence M description 326 source MCSA : MCSA1 15) chain A residue 120 type catalytic sequence T description 326 source MCSA : MCSA1 16) chain A residue 270 type catalytic sequence I description 326 source MCSA : MCSA1 17) chain A residue 328 type catalytic sequence Q description 326 source MCSA : MCSA1 18) chain A residue 70 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 432 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 464 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 482 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 489 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 516 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 75 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 77 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 106 type BINDING sequence P description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 113 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 114 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 120 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 30) chain A residue 207 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 272 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 105 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI11 33) chain A residue 175 type MOD_RES sequence V description Phosphotyrosine => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI11 34) chain A residue 73 type BINDING sequence M description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 270 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 295 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 296 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 328 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 270 type SITE sequence I description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 37 type MOD_RES sequence A description Phosphoserine => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI6 41) chain A residue 148 type MOD_RES sequence M description Phosphotyrosine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 42) chain A residue 166 type MOD_RES sequence V description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI13 43) chain A residue 322 type MOD_RES sequence P description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI13 44) chain A residue 266 type MOD_RES sequence I description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI14 45) chain A residue 270 type MOD_RES sequence I description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI15 46) chain A residue 475 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI16 47) chain A residue 115 type CROSSLNK sequence G description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI17 48) chain A residue 266 type CROSSLNK sequence I description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI18 49) chain A residue 270 type CROSSLNK sequence I description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI18 50) chain A residue 166 type CROSSLNK sequence V description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI19 51) chain A residue 41 type MOD_RES sequence A description Phosphothreonine => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI7 52) chain A residue 195 type MOD_RES sequence E description Phosphothreonine => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI7 53) chain A residue 62 type MOD_RES sequence E description N6-acetyllysine => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI8 54) chain A residue 89 type MOD_RES sequence N description N6-acetyllysine => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI8 55) chain A residue 305 type MOD_RES sequence V description N6-acetyllysine => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI8 56) chain A residue 264-276 type prosite sequence IKIISKIENHEGV description PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV source prosite : PS00110 57) chain A residue 97 type MOD_RES sequence F description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI10 58) chain A residue 100 type MOD_RES sequence D description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI10 59) chain A residue 66 type MOD_RES sequence S description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI9 60) chain A residue 498 type MOD_RES sequence A description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI9

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