eF-site ID 6nn7-A PDB Code 6nn7 Chain A click to enlarge Title The structure of human liver pyruvate kinase, hLPYK-GGG Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence A:  LTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAAR STSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEY HAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGI LQSEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRV VPVGGRIYIDDGLISLVVQKIGLVTQVENGGVLGSRKGVN LPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASD VAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGI MVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQM LESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNF PVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTE VTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAV IAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRV QFGIESGKLRGFLRVGDLVIVVTGWYTNIMRVLSIS Description Functional site 1) chain A residue 333 type sequence G description binding site for residue EDO A 601 source : AC1 2) chain A residue 335 type sequence P description binding site for residue EDO A 601 source : AC1 3) chain A residue 369 type sequence D description binding site for residue EDO A 601 source : AC1 4) chain A residue 451 type sequence Q description binding site for residue EDO A 601 source : AC1 5) chain A residue 454 type sequence S description binding site for residue EDO A 601 source : AC1 6) chain A residue 455 type sequence R description binding site for residue EDO A 601 source : AC1 7) chain A residue 457 type sequence R description binding site for residue EDO A 601 source : AC1 8) chain A residue 478 type sequence C description binding site for residue EDO A 601 source : AC1 9) chain A residue 278 type sequence K description binding site for residue EDO A 602 source : AC2 10) chain A residue 451 type sequence Q description binding site for residue EDO A 602 source : AC2 11) chain A residue 474 type sequence Q description binding site for residue EDO A 602 source : AC2 12) chain A residue 475 type sequence V description binding site for residue EDO A 602 source : AC2 13) chain A residue 444 type sequence T description binding site for residue GOL A 603 source : AC3 14) chain A residue 445 type sequence T description binding site for residue GOL A 603 source : AC3 15) chain A residue 446 type sequence T description binding site for residue GOL A 603 source : AC3 16) chain A residue 448 type sequence R description binding site for residue GOL A 603 source : AC3 17) chain A residue 449 type sequence S description binding site for residue GOL A 603 source : AC3 18) chain A residue 85 type sequence R description binding site for residue GOL A 604 source : AC4 19) chain A residue 282 type sequence K description binding site for residue GOL A 604 source : AC4 20) chain A residue 305 type sequence A description binding site for residue GOL A 604 source : AC4 21) chain A residue 307 type sequence G description binding site for residue GOL A 604 source : AC4 22) chain A residue 308 type sequence D description binding site for residue GOL A 604 source : AC4 23) chain A residue 340 type sequence T description binding site for residue GOL A 604 source : AC4 24) chain A residue 543 type sequence S description binding site for residue GOL E 603 source : AE2 25) chain A residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 26) chain A residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 27) chain A residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 28) chain A residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 29) chain A residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 30) chain A residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 31) chain A residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 32) chain A residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 33) chain A residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 34) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 35) chain A residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 36) chain A residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 37) chain A residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 38) chain A residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 39) chain A residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 40) chain A residue 277-289 type prosite sequence IKIISKIENHEGV description PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV source prosite : PS00110 41) chain A residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 42) 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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