eF-site ID 6nn7-E PDB Code 6nn7 Chain E click to enlarge Title The structure of human liver pyruvate kinase, hLPYK-GGG Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence E:  FQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIG PASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVR EAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEV ELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGG RIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLP GAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVA AVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMV ARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLE SMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPV EAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVT AIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIA VTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQF GIESGKLRGFLRVGDLVIVVTGWRGGGYTNIMRVLSIS Description Functional site 1) chain E residue 275 type sequence H description binding site for residue FLC C 601 source : AC9 2) chain E residue 137 type sequence Q description binding site for residue EDO E 601 source : AD9 3) chain E residue 144 type sequence V description binding site for residue EDO E 601 source : AD9 4) chain E residue 164 type sequence G description binding site for residue EDO E 601 source : AD9 5) chain E residue 165 type sequence N description binding site for residue EDO E 601 source : AD9 6) chain E residue 261 type sequence S description binding site for residue EDO E 602 source : AE1 7) chain E residue 291 type sequence R description binding site for residue EDO E 602 source : AE1 8) chain E residue 93 type sequence H description binding site for residue GOL E 603 source : AE2 9) chain E residue 243 type sequence F description binding site for residue GOL E 603 source : AE2 10) chain E residue 247 type sequence H description binding site for residue GOL E 603 source : AE2 11) chain E residue 421 type sequence T description binding site for residue GOL E 604 source : AE3 12) chain E residue 444 type sequence T description binding site for residue GOL E 604 source : AE3 13) chain E residue 445 type sequence T description binding site for residue GOL E 604 source : AE3 14) chain E residue 446 type sequence T description binding site for residue GOL E 604 source : AE3 15) chain E residue 448 type sequence R description binding site for residue GOL E 604 source : AE3 16) chain E residue 449 type sequence S description binding site for residue GOL E 604 source : AE3 17) chain E residue 534 type sequence T description binding site for residue GOL E 604 source : AE3 18) chain E residue 85 type sequence R description binding site for residue GOL E 605 source : AE4 19) chain E residue 282 type sequence K description binding site for residue GOL E 605 source : AE4 20) chain E residue 305 type sequence A description binding site for residue GOL E 605 source : AE4 21) chain E residue 307 type sequence G description binding site for residue GOL E 605 source : AE4 22) chain E residue 308 type sequence D description binding site for residue GOL E 605 source : AE4 23) chain E residue 340 type sequence T description binding site for residue GOL E 605 source : AE4 24) chain E residue 142 type sequence S description binding site for residue EDO D 602 source : AE6 25) chain E residue 143 type sequence E description binding site for residue EDO D 602 source : AE6 26) chain E residue 144 type sequence V description binding site for residue EDO D 602 source : AE6 27) chain E residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 28) chain E residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 29) chain E residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 30) chain E residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 31) chain E residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 32) chain E residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 33) chain E residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 34) chain E residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 35) chain E residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 36) chain E residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 37) chain E residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 38) chain E residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 39) chain E residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 40) chain E residue 528 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 41) chain E residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 42) chain E residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 43) chain E residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 44) chain E residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

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