eF-site ID 6nn7-G PDB Code 6nn7 Chain G click to enlarge Title The structure of human liver pyruvate kinase, hLPYK-GGG Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence G:  QLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAA RSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHE YHAESIANVREAVESFAYRPVAIALDTKGPEIRTGIELVK GSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYI DDGLISLVVQKIGPLVTQVENGGRKGVNLPLSEQDVRDLR FGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISK IENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQ KMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVAN AVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVY HRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIV LTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVF PLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVI VVTGWYTNIMRVLSIS Description Functional site 1) chain G residue 541 type sequence S description binding site for residue EDO C 602 source : AD1 2) chain G residue 543 type sequence S description binding site for residue EDO C 602 source : AD1 3) chain G residue 85 type sequence R description binding site for residue EDO G 601 source : AF2 4) chain G residue 305 type sequence A description binding site for residue EDO G 601 source : AF2 5) chain G residue 307 type sequence G description binding site for residue EDO G 601 source : AF2 6) chain G residue 308 type sequence D description binding site for residue EDO G 601 source : AF2 7) chain G residue 340 type sequence T description binding site for residue EDO G 601 source : AF2 8) chain G residue 333 type sequence G description binding site for residue EDO G 602 source : AF3 9) chain G residue 334 type sequence K description binding site for residue EDO G 602 source : AF3 10) chain G residue 335 type sequence P description binding site for residue EDO G 602 source : AF3 11) chain G residue 369 type sequence D description binding site for residue EDO G 602 source : AF3 12) chain G residue 454 type sequence S description binding site for residue EDO G 602 source : AF3 13) chain G residue 455 type sequence R description binding site for residue EDO G 602 source : AF3 14) chain G residue 457 type sequence R description binding site for residue EDO G 602 source : AF3 15) chain G residue 478 type sequence C description binding site for residue EDO G 602 source : AF3 16) chain G residue 444 type sequence T description binding site for residue GOL G 603 source : AF4 17) chain G residue 445 type sequence T description binding site for residue GOL G 603 source : AF4 18) chain G residue 446 type sequence T description binding site for residue GOL G 603 source : AF4 19) chain G residue 448 type sequence R description binding site for residue GOL G 603 source : AF4 20) chain G residue 449 type sequence S description binding site for residue GOL G 603 source : AF4 21) chain G residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 22) chain G residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 23) chain G residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 24) chain G residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 25) chain G residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 26) chain G residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 27) chain G residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 28) chain G residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 29) chain G residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 30) chain G residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 31) chain G residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 32) chain G residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 33) chain G residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 34) chain G residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 35) chain G residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 36) chain G residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 37) chain G residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

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