eF-site ID 6nn8-G PDB Code 6nn8 Chain G click to enlarge Title The structure of human liver pyruvate kinase, hLPYK-S531E Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence G:  LGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSI IATIGPASRSVERLKEMIKAGMNIARLNFSEYHAESIANV REAVESFAGSYRPVAIALDTKGPEDIVFASFVRKASDVAA VRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVA RGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLES MITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVE AVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTA IGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAV TRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFG IESGKLRGFLRVGDLVIVVTGWRPYTNIMRVLSIS Description Functional site 1) chain G residue 28 type sequence Q description binding site for residue EDO G 601 source : AG1 2) chain G residue 51 type sequence P description binding site for residue EDO G 601 source : AG1 3) chain G residue 52 type sequence V description binding site for residue EDO G 601 source : AG1 4) chain G residue 53 type sequence A description binding site for residue EDO G 601 source : AG1 5) chain G residue 395 type sequence R description binding site for residue EDO G 601 source : AG1 6) chain G residue 398 type sequence E description binding site for residue EDO G 601 source : AG1 7) chain G residue 399 type sequence A description binding site for residue EDO G 601 source : AG1 8) chain G residue 404 type sequence R description binding site for residue EDO G 602 source : AG2 9) chain G residue 459 type sequence R description binding site for residue EDO G 602 source : AG2 10) chain G residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 11) chain G residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 12) chain G residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 13) chain G residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 14) chain G residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 15) chain G residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 16) chain G residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 17) chain G residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 18) chain G residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 19) chain G residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 20) chain G residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 21) chain G residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 22) chain G residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 23) chain G residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 24) chain G residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 25) chain G residue 528 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2

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