eF-site ID 6nn8-A PDB Code 6nn8 Chain A click to enlarge Title The structure of human liver pyruvate kinase, hLPYK-S531E Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence A:  LGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSI IATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAES IANVREAVESFAGSPLSYRPVAIALDTKGPEIRTVELVKG SQVLVTNANTVWVDYPNIVRVVPVGGRIYIDDGLISLVVQ KIGPEGLVTQVENGGVLGSRKGVNLPGAQVDLPGLSEQDV RDLRFGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIK IISKIENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKV FLAQKMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETS DVANAVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAE AAVYHRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAA AIIVLTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLC RGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVG DLVIVVTGWRPGEGYTNIMRVLSIS Description Functional site 1) chain A residue 58 type sequence S description binding site for residue EDO A 601 source : AC1 2) chain A residue 82 type sequence N description binding site for residue EDO A 601 source : AC1 3) chain A residue 476 type sequence H description binding site for residue EDO A 601 source : AC1 4) chain A residue 481 type sequence V description binding site for residue EDO A 601 source : AC1 5) chain A residue 482 type sequence F description binding site for residue EDO A 601 source : AC1 6) chain A residue 93 type sequence H description binding site for residue EDO A 602 source : AC2 7) chain A residue 239 type sequence R description binding site for residue EDO A 602 source : AC2 8) chain A residue 68 type sequence R description binding site for residue EDO A 603 source : AC3 9) chain A residue 69 type sequence S description binding site for residue EDO A 603 source : AC3 10) chain A residue 102 type sequence N description binding site for residue EDO A 603 source : AC3 11) chain A residue 107 type sequence V description binding site for residue EDO A 604 source : AC4 12) chain A residue 110 type sequence F description binding site for residue EDO A 604 source : AC4 13) chain A residue 116 type sequence S description binding site for residue EDO A 604 source : AC4 14) chain A residue 117 type sequence Y description binding site for residue EDO A 604 source : AC4 15) chain A residue 118 type sequence R description binding site for residue EDO A 604 source : AC4 16) chain A residue 85 type sequence R description binding site for residue EDO A 605 source : AC5 17) chain A residue 305 type sequence A description binding site for residue EDO A 605 source : AC5 18) chain A residue 308 type sequence D description binding site for residue EDO A 605 source : AC5 19) chain A residue 278 type sequence K description binding site for residue EDO A 606 source : AC6 20) chain A residue 451 type sequence Q description binding site for residue EDO A 606 source : AC6 21) chain A residue 474 type sequence Q description binding site for residue EDO A 606 source : AC6 22) chain A residue 245 type sequence V description binding site for residue EDO A 607 source : AC7 23) chain A residue 248 type sequence G description binding site for residue EDO A 607 source : AC7 24) chain A residue 249 type sequence V description binding site for residue EDO A 607 source : AC7 25) chain A residue 273 type sequence E description binding site for residue EDO A 607 source : AC7 26) chain A residue 470 type sequence Q description binding site for residue EDO A 607 source : AC7 27) chain A residue 333 type sequence G description binding site for residue EDO A 608 source : AC8 28) chain A residue 334 type sequence K description binding site for residue EDO A 608 source : AC8 29) chain A residue 335 type sequence P description binding site for residue EDO A 608 source : AC8 30) chain A residue 369 type sequence D description binding site for residue EDO A 608 source : AC8 31) chain A residue 455 type sequence R description binding site for residue EDO A 608 source : AC8 32) chain A residue 457 type sequence R description binding site for residue EDO A 608 source : AC8 33) chain A residue 539 type sequence V description binding site for residue EDO A 609 source : AC9 34) chain A residue 541 type sequence S description binding site for residue EDO A 609 source : AC9 35) chain A residue 65 type sequence P description binding site for residue EDO A 610 source : AD1 36) chain A residue 66 type sequence A description binding site for residue EDO A 610 source : AD1 37) chain A residue 69 type sequence S description binding site for residue EDO A 610 source : AD1 38) chain A residue 72 type sequence R description binding site for residue EDO A 610 source : AD1 39) chain A residue 46 type sequence D description binding site for residue EDO B 606 source : AD7 40) chain A residue 420 type sequence P description binding site for residue EDO D 602 source : AE7 41) chain A residue 277-289 type prosite sequence IKIISKIENHEGV description PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV source prosite : PS00110 42) chain A residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 43) chain A residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 44) chain A residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 45) chain A residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 46) chain A residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 47) chain A residue 528 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 48) chain A residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 49) chain A residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 50) chain A residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 51) chain A residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 52) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 53) chain A residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 54) chain A residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 55) chain A residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 56) chain A residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 58) chain A residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 59) chain A residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

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