eF-site ID 4qgc-A PDB Code 4qgc Chain A click to enlarge Title crystal structure of PKM2-K422R mutant Classification TRANSFERASE Compound Pyruvate kinase PKM Source Homo sapiens (Human) (KPYM_HUMAN) Sequence A:  DTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPI LYRPVAVALDTKGPEIRTGLIKGTAEVELKKGATLKITLD NAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQV KQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKD IQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNI KIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEK VFLAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEG SDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREA EAAIYHLQLFEELRRLAPDPTEATAVGAVEASFRCCSGAI IVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRG IFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDV VIVLTGWRPGSGFTNTMRVVPVP Description Functional site 1) chain A residue 75 type sequence N description BINDING SITE FOR RESIDUE K A 1001 source : AC1 2) chain A residue 77 type sequence S description BINDING SITE FOR RESIDUE K A 1001 source : AC1 3) chain A residue 113 type sequence D description BINDING SITE FOR RESIDUE K A 1001 source : AC1 4) chain A residue 114 type sequence T description BINDING SITE FOR RESIDUE K A 1001 source : AC1 5) chain A residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC2 6) chain A residue 482 type sequence W description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC2 7) chain A residue 489 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1002 source : AC2 8) chain A residue 432 type sequence T description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 9) chain A residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 10) chain A residue 434 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 11) chain A residue 435 type sequence G description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 12) chain A residue 436 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 13) chain A residue 437 type sequence S description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 14) chain A residue 522 type sequence T description BINDING SITE FOR RESIDUE SO4 A 1003 source : AC3 15) chain A residue 75 type sequence N description BINDING SITE FOR RESIDUE SO4 A 1004 source : AC4 16) chain A residue 78 type sequence H description BINDING SITE FOR RESIDUE SO4 A 1004 source : AC4 17) chain A residue 120 type sequence R description BINDING SITE FOR RESIDUE SO4 A 1004 source : AC4 18) chain A residue 43 type sequence R description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 19) chain A residue 44 type sequence N description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 20) chain A residue 70 type sequence N description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 21) chain A residue 106 type sequence R description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 22) chain A residue 464 type sequence H description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 23) chain A residue 470 type sequence F description BINDING SITE FOR RESIDUE GOL A 1005 source : AC5 24) chain A residue 70 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 106 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 464 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 41 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 28) chain A residue 62 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 29) chain A residue 89 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 30) chain A residue 305 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21700219 source Swiss-Prot : SWS_FT_FI22 31) chain A residue 403 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 32) chain A residue 408 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 33) chain A residue 433 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI24 34) chain A residue 265-277 type prosite sequence IKIISKIENHEGV description PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV source prosite : PS00110 35) chain A residue 266 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 36) chain A residue 270 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI27 37) chain A residue 475 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI25 38) chain A residue 115 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI26 39) chain A residue 166 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI28 40) chain A residue 66 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 41) chain A residue 498 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 42) chain A residue 97 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 43) chain A residue 100 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 44) chain A residue 105 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 45) chain A residue 148 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI16 46) chain A residue 166 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 47) chain A residue 322 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 48) chain A residue 175 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI18 49) chain A residue 432 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 50) chain A residue 482 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 51) chain A residue 489 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 52) chain A residue 516 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI4 53) chain A residue 270 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI5 54) chain A residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 55) chain A residue 73 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 56) chain A residue 270 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 57) chain A residue 295 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 296 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 59) chain A residue 328 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 60) chain A residue 266 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 61) chain A residue 270 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI21 62) chain A residue 75 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 63) chain A residue 77 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 64) chain A residue 113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 65) chain A residue 114 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 66) chain A residue 120 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 67) chain A residue 207 type BINDING sequence K description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 68) chain A residue 272 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 69) chain A residue 433 type SITE sequence K description Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445 source Swiss-Prot : SWS_FT_FI6 70) chain A residue 37 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

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