eF-site ID 6nn8-C PDB Code 6nn8 Chain C click to enlarge Title The structure of human liver pyruvate kinase, hLPYK-S531E Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence C:  QELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARST SIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHA ESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGIEV ELVKGSQVLVTVANTVWVDYPNIVRVVPVGGRIYIDDGLI SLVVQKILVTQVENGGVLGSRKGVNLPGLSEQDVRDLRFG VEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIE NHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKM MIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAV LDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHR QLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLT TTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPL LYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVV TGWRPGEGYTNIMRVLSIS Description Functional site 1) chain C residue 443 type sequence L description binding site for residue EDO C 601 source : AD9 2) chain C residue 445 type sequence T description binding site for residue EDO C 601 source : AD9 3) chain C residue 494 type sequence W description binding site for residue EDO C 601 source : AD9 4) chain C residue 501 type sequence R description binding site for residue EDO C 601 source : AD9 5) chain C residue 530 type sequence G description binding site for residue EDO C 601 source : AD9 6) chain C residue 531 type sequence E description binding site for residue EDO C 601 source : AD9 7) chain C residue 85 type sequence R description binding site for residue EDO C 602 source : AE1 8) chain C residue 305 type sequence A description binding site for residue EDO C 602 source : AE1 9) chain C residue 307 type sequence G description binding site for residue EDO C 602 source : AE1 10) chain C residue 308 type sequence D description binding site for residue EDO C 602 source : AE1 11) chain C residue 340 type sequence T description binding site for residue EDO C 602 source : AE1 12) chain C residue 55 type sequence R description binding site for residue EDO C 603 source : AE2 13) chain C residue 58 type sequence S description binding site for residue EDO C 603 source : AE2 14) chain C residue 82 type sequence N description binding site for residue EDO C 603 source : AE2 15) chain C residue 476 type sequence H description binding site for residue EDO C 603 source : AE2 16) chain C residue 481 type sequence V description binding site for residue EDO C 603 source : AE2 17) chain C residue 482 type sequence F description binding site for residue EDO C 603 source : AE2 18) chain C residue 267 type sequence R description binding site for residue EDO C 604 source : AE3 19) chain C residue 298 type sequence V description binding site for residue EDO C 604 source : AE3 20) chain C residue 299 type sequence S description binding site for residue EDO C 604 source : AE3 21) chain C residue 300 type sequence D description binding site for residue EDO C 604 source : AE3 22) chain C residue 334 type sequence K description binding site for residue EDO C 604 source : AE3 23) chain C residue 278 type sequence K description binding site for residue EDO C 605 source : AE4 24) chain C residue 447 type sequence G description binding site for residue EDO C 605 source : AE4 25) chain C residue 451 type sequence Q description binding site for residue EDO C 605 source : AE4 26) chain C residue 474 type sequence Q description binding site for residue EDO C 605 source : AE4 27) chain C residue 381 type sequence N description binding site for residue EDO C 606 source : AE5 28) chain C residue 382 type sequence F description binding site for residue EDO C 606 source : AE5 29) chain C residue 383 type sequence P description binding site for residue EDO C 606 source : AE5 30) chain C residue 384 type sequence V description binding site for residue EDO C 606 source : AE5 31) chain C residue 385 type sequence E description binding site for residue EDO C 606 source : AE5 32) chain C residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 33) chain C residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 34) chain C residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 35) chain C residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 36) chain C residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 37) chain C residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 38) chain C residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 39) chain C residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 40) chain C residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 41) chain C residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 42) chain C residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 43) chain C residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 44) chain C residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 45) chain C residue 528 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 46) chain C residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 47) chain C residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 48) chain C residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 49) chain C residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

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