eF-site ID 6nn8-D PDB Code 6nn8 Chain D click to enlarge Title The structure of human liver pyruvate kinase, hLPYK-S531E Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence D:  VAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPV AARSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSSHE YHAESIANVREAVESFAGSPLSYRPVAIALDTKGPVRDLR FGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISK IENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQ KMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVAN AVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVY HRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIV LTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVF PLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVI VVTGWRPGEGYTNIMRVLSIS Description Functional site 1) chain D residue 420 type sequence P description binding site for residue EDO A 609 source : AC9 2) chain D residue 535 type sequence N description binding site for residue EDO A 609 source : AC9 3) chain D residue 85 type sequence R description binding site for residue EDO D 601 source : AE6 4) chain D residue 282 type sequence K description binding site for residue EDO D 601 source : AE6 5) chain D residue 284 type sequence E description binding site for residue EDO D 601 source : AE6 6) chain D residue 307 type sequence G description binding site for residue EDO D 601 source : AE6 7) chain D residue 308 type sequence D description binding site for residue EDO D 601 source : AE6 8) chain D residue 340 type sequence T description binding site for residue EDO D 601 source : AE6 9) chain D residue 539 type sequence V description binding site for residue EDO D 602 source : AE7 10) chain D residue 541 type sequence S description binding site for residue EDO D 602 source : AE7 11) chain D residue 28 type sequence Q description binding site for residue EDO D 603 source : AE8 12) chain D residue 53 type sequence A description binding site for residue EDO D 603 source : AE8 13) chain D residue 437 type sequence A description binding site for residue EDO D 603 source : AE8 14) chain D residue 438 type sequence A description binding site for residue EDO D 603 source : AE8 15) chain D residue 459 type sequence R description binding site for residue EDO D 603 source : AE8 16) chain D residue 460 type sequence A description binding site for residue EDO D 603 source : AE8 17) chain D residue 461 type sequence A description binding site for residue EDO D 603 source : AE8 18) chain D residue 495 type sequence A description binding site for residue EDO D 604 source : AE9 19) chain D residue 498 type sequence V description binding site for residue EDO D 604 source : AE9 20) chain D residue 525 type sequence T description binding site for residue EDO D 604 source : AE9 21) chain D residue 526 type sequence G description binding site for residue EDO D 604 source : AE9 22) chain D residue 536 type sequence I description binding site for residue EDO D 604 source : AE9 23) chain D residue 538 type sequence R description binding site for residue EDO D 604 source : AE9 24) chain D residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 25) chain D residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 26) chain D residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 27) chain D residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 28) chain D residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 29) chain D residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 30) chain D residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 31) chain D residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 32) chain D residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 33) chain D residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 34) chain D residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 35) chain D residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 36) chain D residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 37) chain D residue 528 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 38) chain D residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 39) chain D residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

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