eF-site ID 4qgc-D PDB Code 4qgc Chain D click to enlarge Title crystal structure of PKM2-K422R mutant Classification TRANSFERASE Compound Pyruvate kinase PKM Source Homo sapiens (Human) (KPYM_HUMAN) Sequence D:  TFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEM IKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPIL YRPVAVALDTKGPEIRTGLIKGAEVELKKGATLKITLDNA YMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQ KGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQ DLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKI ISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVF LAQKMMIGRCNRAGKPVICATQMLESMIKKPRPTRAEGSD VANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAREAEA AIYHLQLFEELRRLSDPTEATAVGAVEASFRCCSGAIIVL TKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFP VLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIV LTGWRPGSGFTNTMRVVPVP Description Functional site 1) chain D residue 75 type sequence N description BINDING SITE FOR RESIDUE K D 1001 source : BC5 2) chain D residue 77 type sequence S description BINDING SITE FOR RESIDUE K D 1001 source : BC5 3) chain D residue 113 type sequence D description BINDING SITE FOR RESIDUE K D 1001 source : BC5 4) chain D residue 114 type sequence T description BINDING SITE FOR RESIDUE K D 1001 source : BC5 5) chain D residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1002 source : BC6 6) chain D residue 482 type sequence W description BINDING SITE FOR RESIDUE SO4 D 1002 source : BC6 7) chain D residue 489 type sequence R description BINDING SITE FOR RESIDUE SO4 D 1002 source : BC6 8) chain D residue 432 type sequence T description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 9) chain D residue 433 type sequence K description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 10) chain D residue 434 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 11) chain D residue 436 type sequence R description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 12) chain D residue 437 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1003 source : BC7 13) chain D residue 43 type sequence R description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 14) chain D residue 44 type sequence N description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 15) chain D residue 70 type sequence N description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 16) chain D residue 106 type sequence R description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 17) chain D residue 464 type sequence H description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 18) chain D residue 469 type sequence I description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 19) chain D residue 470 type sequence F description BINDING SITE FOR RESIDUE GOL D 1004 source : BC8 20) chain D residue 70 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 21) chain D residue 106 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 22) chain D residue 464 type BINDING sequence H description BINDING => ECO:0000269|PubMed:23064226 source Swiss-Prot : SWS_FT_FI1 23) chain D residue 41 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 24) chain D residue 62 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 25) chain D residue 89 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI11 26) chain D residue 305 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:21700219 source Swiss-Prot : SWS_FT_FI22 27) chain D residue 408 type MOD_RES sequence P description 4-hydroxyproline => ECO:0000269|PubMed:21620138 source Swiss-Prot : SWS_FT_FI23 28) chain D 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 29) chain D 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 30) chain D 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 31) chain D residue 475 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI25 32) chain D 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 33) chain D 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 34) chain D residue 66 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 35) chain D residue 498 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI12 36) chain D residue 97 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 37) chain D residue 100 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P11980 source Swiss-Prot : SWS_FT_FI13 38) chain D residue 105 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI14 39) chain D residue 148 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI16 40) chain D residue 166 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 41) chain D residue 322 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI17 42) chain D residue 175 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI18 43) chain D 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 44) chain D 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 45) chain D 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 46) chain D 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 47) chain D residue 270 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI5 48) chain D residue 195 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19690332 source Swiss-Prot : SWS_FT_FI19 49) chain D residue 73 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 50) chain D residue 270 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 51) chain D residue 295 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 52) chain D residue 296 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 53) chain D residue 328 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P30613 source Swiss-Prot : SWS_FT_FI2 54) chain D residue 266 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI20 55) chain D residue 270 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 source Swiss-Prot : SWS_FT_FI21 56) chain D residue 75 type BINDING sequence N description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 57) chain D residue 77 type BINDING sequence S description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 58) chain D residue 113 type BINDING sequence D description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 59) chain D residue 114 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 60) chain D residue 120 type BINDING sequence R description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 61) chain D residue 207 type BINDING sequence K description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 62) chain D residue 272 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF source Swiss-Prot : SWS_FT_FI3 63) chain D residue 433 type SITE sequence K description Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445 source Swiss-Prot : SWS_FT_FI6 64) chain D 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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