eF-site ID 6nn7-H PDB Code 6nn7 Chain H click to enlarge Title The structure of human liver pyruvate kinase, hLPYK-GGG Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence H:  QQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPA SRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREA VESFSPLSYRPVAIALDTKGPSEQDVRDLRFGVEHGVDIV FASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRF DEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLA GKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIM LSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRR AAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQL LSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPAD DVDRRVQFGIESGKLRGFLRVGDLVIVVTTNIMRVLSI Description Functional site 1) chain H residue 85 type sequence R description binding site for residue GOL H 601 source : AF5 2) chain H residue 282 type sequence K description binding site for residue GOL H 601 source : AF5 3) chain H residue 284 type sequence E description binding site for residue GOL H 601 source : AF5 4) chain H residue 305 type sequence A description binding site for residue GOL H 601 source : AF5 5) chain H residue 307 type sequence G description binding site for residue GOL H 601 source : AF5 6) chain H residue 308 type sequence D description binding site for residue GOL H 601 source : AF5 7) chain H residue 340 type sequence T description binding site for residue GOL H 601 source : AF5 8) chain H residue 444 type sequence T description binding site for residue GOL H 602 source : AF6 9) chain H residue 445 type sequence T description binding site for residue GOL H 602 source : AF6 10) chain H residue 446 type sequence T description binding site for residue GOL H 602 source : AF6 11) chain H residue 449 type sequence S description binding site for residue GOL H 602 source : AF6 12) chain H residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 13) chain H residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 14) chain H residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 15) chain H residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 16) chain H residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 17) chain H residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 18) chain H residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 19) chain H residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 20) chain H residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 21) chain H residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 22) chain H residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 23) chain H residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 24) chain H residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 25) chain H residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

Display surface Download Links