eF-site ID 6nn7-ABCDEFGH PDB Code 6nn7 Chain A, B, C, D, E, F, G, H Title The structure of human liver pyruvate kinase, hLPYK-GGG Classification TRANSFERASE Compound Pyruvate kinase PKLR Source (KPYR_HUMAN) Sequence A:  LTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAAR STSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHEY HAESIANVREAVESFAGSPLSYRPVAIALDTKGPEIRTGI LQSEVELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRV VPVGGRIYIDDGLISLVVQKIGLVTQVENGGVLGSRKGVN LPGAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASD VAAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGI MVARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQM LESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNF PVEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTE VTAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAV IAVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRV QFGIESGKLRGFLRVGDLVIVVTGWYTNIMRVLSIS B:  QQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGP ASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVRE AVESFAGSPLSYRPVAIALDTKGPEIRGLSEQDVRDLRFG VEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISKIE NHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKM MIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVANAV LDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHR QLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLT TTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPL LYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVV TGWYTNIMRVLSIS C:  QQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPA SRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREA VESFAGSPYRPVAIALDTKGPEIRTGILQGGPESEVELVK GSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYI DDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLPGAQV DLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVAAVRA ALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMVARGD LGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLESMIT KPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPVEAVK MQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVTAIGA VEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIAVTRS AQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQFGIES GKLRGFLRVGDLVIVVTGWRGGGYTNIMRVLSIS D:  AFFQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIAT IGPASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIAN VREAVESFAGSPLSYRPVAIALDTKGPEIRTGSEVELVKL VTVDPRGNANTVWVDYPNIVVPIYIDDGLISLQKINGGVL GSRKGVNLPLSEQDVRDLRFGVEHGVDIVFASFVRKASDV AAVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIM VARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQML ESMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFP VEAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEV TAIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVI AVTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQ FGIESGKLRGFLRVGDLVIVVTGWRGGGYTNIMRVLSIS E:  FQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIG PASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVR EAVESFAGSPLSYRPVAIALDTKGPEIRTGILQGGPESEV ELVKGSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGG RIYIDDGLISLVVQKIGPEGLVTQVENGGVLGSRKGVNLP GAQVDLPGLSEQDVRDLRFGVEHGVDIVFASFVRKASDVA AVRAALGPEGHGIKIISKIENHEGVKRFDEILEVSDGIMV ARGDLGIEIPAEKVFLAQKMMIGRCNLAGKPVVCATQMLE SMITKPRPTRAETSDVANAVLDGADCIMLSGETAKGNFPV EAVKMQHAIAREAEAAVYHRQLFEELRRAAPLSRDPTEVT AIGAVEAAFKCCAAAIIVLTTTGRSAQLLSRYRPRAAVIA VTRSAQAARQVHLCRGVFPLLYREPPEAIWADDVDRRVQF GIESGKLRGFLRVGDLVIVVTGWRGGGYTNIMRVLSIS F:  FQQQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIG PASRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVR EAVESFASYRPVAIALDTKGPEILSEQDVRDLRFGVEHGV DIVFASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGV KRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRC NLAGKPVVCATQMLESMITKPRPTRAETSDVANAVLDGAD CIMLSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEE LRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRS AQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREP PEAIWADDVDRRVQFGIESGKLRGFLRVGDLVIVVTTNIM RVLSIS G:  QLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSEPVAA RSTSIIATIGPASRSVERLKEMIKAGMNIARLNFSHGSHE YHAESIANVREAVESFAYRPVAIALDTKGPEIRTGIELVK GSQVLVTVDPAFRTRGNANTVWVDYPNIVRVVPVGGRIYI DDGLISLVVQKIGPLVTQVENGGRKGVNLPLSEQDVRDLR FGVEHGVDIVFASFVRKASDVAAVRAALGPEGHGIKIISK IENHEGVKRFDEILEVSDGIMVARGDLGIEIPAEKVFLAQ KMMIGRCNLAGKPVVCATQMLESMITKPRPTRAETSDVAN AVLDGADCIMLSGETAKGNFPVEAVKMQHAIAREAEAAVY HRQLFEELRRAAPLSRDPTEVTAIGAVEAAFKCCAAAIIV LTTTGRSAQLLSRYRPRAAVIAVTRSAQAARQVHLCRGVF PLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRVGDLVI VVTGWYTNIMRVLSIS H:  QQQLPAAMADTFLEHLCLLDIDSEPVAARSTSIIATIGPA SRSVERLKEMIKAGMNIARLNFSHGSHEYHAESIANVREA VESFSPLSYRPVAIALDTKGPSEQDVRDLRFGVEHGVDIV FASFVRKASDVAAVRAALGPEGHGIKIISKIENHEGVKRF DEILEVSDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNLA GKPVVCATQMLESMITKPRPTRAETSDVANAVLDGADCIM LSGETAKGNFPVEAVKMQHAIAREAEAAVYHRQLFEELRR AAPLSRDPTEVTAIGAVEAAFKCCAAAIIVLTTTGRSAQL LSRYRPRAAVIAVTRSAQAARQVHLCRGVFPLLYREPPAD DVDRRVQFGIESGKLRGFLRVGDLVIVVTTNIMRVLSI Description Functional site 1) chain A residue 333 type sequence G description binding site for residue EDO A 601 source : AC1 2) chain A residue 335 type sequence P description binding site for residue EDO A 601 source : AC1 3) chain A residue 369 type sequence D description binding site for residue EDO A 601 source : AC1 4) chain A residue 451 type sequence Q description binding site for residue EDO A 601 source : AC1 5) chain A residue 454 type sequence S description binding site for residue EDO A 601 source : AC1 6) chain A residue 455 type sequence R description binding site for residue EDO A 601 source : AC1 7) chain A residue 457 type sequence R description binding site for residue EDO A 601 source : AC1 8) chain A residue 478 type sequence C description binding site for residue EDO A 601 source : AC1 9) chain A residue 278 type sequence K description binding site for residue EDO A 602 source : AC2 10) chain A residue 451 type sequence Q description binding site for residue EDO A 602 source : AC2 11) chain A residue 474 type sequence Q description binding site for residue EDO A 602 source : AC2 12) chain A residue 475 type sequence V description binding site for residue EDO A 602 source : AC2 13) chain A residue 444 type sequence T description binding site for residue GOL A 603 source : AC3 14) chain A residue 445 type sequence T description binding site for residue GOL A 603 source : AC3 15) chain A residue 446 type sequence T description binding site for residue GOL A 603 source : AC3 16) chain A residue 448 type sequence R description binding site for residue GOL A 603 source : AC3 17) chain A residue 449 type sequence S description binding site for residue GOL A 603 source : AC3 18) chain A residue 85 type sequence R description binding site for residue GOL A 604 source : AC4 19) chain A residue 282 type sequence K description binding site for residue GOL A 604 source : AC4 20) chain A residue 305 type sequence A description binding site for residue GOL A 604 source : AC4 21) chain A residue 307 type sequence G description binding site for residue GOL A 604 source : AC4 22) chain A residue 308 type sequence D description binding site for residue GOL A 604 source : AC4 23) chain A residue 340 type sequence T description binding site for residue GOL A 604 source : AC4 24) chain B residue 333 type sequence G description binding site for residue EDO B 601 source : AC5 25) chain B residue 334 type sequence K description binding site for residue EDO B 601 source : AC5 26) chain B residue 335 type sequence P description binding site for residue EDO B 601 source : AC5 27) chain B residue 369 type sequence D description binding site for residue EDO B 601 source : AC5 28) chain B residue 454 type sequence S description binding site for residue EDO B 601 source : AC5 29) chain B residue 478 type sequence C description binding site for residue EDO B 601 source : AC5 30) chain B residue 278 type sequence K description binding site for residue EDO B 602 source : AC6 31) chain B residue 451 type sequence Q description binding site for residue EDO B 602 source : AC6 32) chain B residue 421 type sequence T description binding site for residue GOL B 603 source : AC7 33) chain B residue 444 type sequence T description binding site for residue GOL B 603 source : AC7 34) chain B residue 445 type sequence T description binding site for residue GOL B 603 source : AC7 35) chain B residue 446 type sequence T description binding site for residue GOL B 603 source : AC7 36) chain B residue 448 type sequence R description binding site for residue GOL B 603 source : AC7 37) chain B residue 449 type sequence S description binding site for residue GOL B 603 source : AC7 38) chain B residue 85 type sequence R description binding site for residue GOL B 604 source : AC8 39) chain B residue 282 type sequence K description binding site for residue GOL B 604 source : AC8 40) chain B residue 284 type sequence E description binding site for residue GOL B 604 source : AC8 41) chain B residue 305 type sequence A description binding site for residue GOL B 604 source : AC8 42) chain B residue 307 type sequence G description binding site for residue GOL B 604 source : AC8 43) chain B residue 308 type sequence D description binding site for residue GOL B 604 source : AC8 44) chain B residue 340 type sequence T description binding site for residue GOL B 604 source : AC8 45) chain C residue 421 type sequence T description binding site for residue FLC C 601 source : AC9 46) chain C residue 444 type sequence T description binding site for residue FLC C 601 source : AC9 47) chain C residue 445 type sequence T description binding site for residue FLC C 601 source : AC9 48) chain C residue 446 type sequence T description binding site for residue FLC C 601 source : AC9 49) chain C residue 448 type sequence R description binding site for residue FLC C 601 source : AC9 50) chain C residue 449 type sequence S description binding site for residue FLC C 601 source : AC9 51) chain C residue 534 type sequence T description binding site for residue FLC C 601 source : AC9 52) chain E residue 275 type sequence H description binding site for residue FLC C 601 source : AC9 53) chain C residue 93 type sequence H description binding site for residue EDO C 602 source : AD1 54) chain C residue 247 type sequence H description binding site for residue EDO C 602 source : AD1 55) chain G residue 541 type sequence S description binding site for residue EDO C 602 source : AD1 56) chain G residue 543 type sequence S description binding site for residue EDO C 602 source : AD1 57) chain C residue 104 type sequence R description binding site for residue EDO C 603 source : AD2 58) chain C residue 122 type sequence I description binding site for residue EDO C 603 source : AD2 59) chain C residue 248 type sequence G description binding site for residue EDO C 603 source : AD2 60) chain C residue 249 type sequence V description binding site for residue EDO C 603 source : AD2 61) chain C residue 250 type sequence D description binding site for residue EDO C 603 source : AD2 62) chain C residue 473 type sequence R description binding site for residue EDO C 603 source : AD2 63) chain C residue 278 type sequence K description binding site for residue EDO C 604 source : AD3 64) chain C residue 451 type sequence Q description binding site for residue EDO C 604 source : AD3 65) chain C residue 474 type sequence Q description binding site for residue EDO C 604 source : AD3 66) chain C residue 306 type sequence R description binding site for residue EDO C 605 source : AD4 67) chain C residue 318 type sequence V description binding site for residue EDO C 605 source : AD4 68) chain C residue 319 type sequence F description binding site for residue EDO C 605 source : AD4 69) chain C residue 322 type sequence Q description binding site for residue EDO C 605 source : AD4 70) chain D residue 354 type sequence R description binding site for residue EDO C 605 source : AD4 71) chain D residue 357 type sequence T description binding site for residue EDO C 605 source : AD4 72) chain C residue 129 type sequence P description binding site for residue EDO C 606 source : AD5 73) chain C residue 221 type sequence V description binding site for residue EDO C 606 source : AD5 74) chain C residue 256 type sequence F description binding site for residue EDO C 606 source : AD5 75) chain C residue 137 type sequence Q description binding site for residue EDO C 607 source : AD6 76) chain C residue 165 type sequence N description binding site for residue EDO C 607 source : AD6 77) chain F residue 71 type sequence E description binding site for residue EDO C 607 source : AD6 78) chain C residue 351 type sequence R description binding site for residue EDO C 608 source : AD7 79) chain C residue 85 type sequence R description binding site for residue GOL C 609 source : AD8 80) chain C residue 282 type sequence K description binding site for residue GOL C 609 source : AD8 81) chain C residue 305 type sequence A description binding site for residue GOL C 609 source : AD8 82) chain C residue 307 type sequence G description binding site for residue GOL C 609 source : AD8 83) chain C residue 308 type sequence D description binding site for residue GOL C 609 source : AD8 84) chain C residue 340 type sequence T description binding site for residue GOL C 609 source : AD8 85) chain D residue 69 type sequence S description binding site for residue EDO E 601 source : AD9 86) chain E residue 137 type sequence Q description binding site for residue EDO E 601 source : AD9 87) chain E residue 144 type sequence V description binding site for residue EDO E 601 source : AD9 88) chain E residue 164 type sequence G description binding site for residue EDO E 601 source : AD9 89) chain E residue 165 type sequence N description binding site for residue EDO E 601 source : AD9 90) chain E residue 261 type sequence S description binding site for residue EDO E 602 source : AE1 91) chain E residue 291 type sequence R description binding site for residue EDO E 602 source : AE1 92) chain A residue 543 type sequence S description binding site for residue GOL E 603 source : AE2 93) chain C residue 528 type sequence R description binding site for residue GOL E 603 source : AE2 94) chain E residue 93 type sequence H description binding site for residue GOL E 603 source : AE2 95) chain E residue 243 type sequence F description binding site for residue GOL E 603 source : AE2 96) chain E residue 247 type sequence H description binding site for residue GOL E 603 source : AE2 97) chain C residue 275 type sequence H description binding site for residue GOL E 604 source : AE3 98) chain E residue 421 type sequence T description binding site for residue GOL E 604 source : AE3 99) chain E residue 444 type sequence T description binding site for residue GOL E 604 source : AE3 100) chain E residue 445 type sequence T description binding site for residue GOL E 604 source : AE3 101) chain E residue 446 type sequence T description binding site for residue GOL E 604 source : AE3 102) chain E residue 448 type sequence R description binding site for residue GOL E 604 source : AE3 103) chain E residue 449 type sequence S description binding site for residue GOL E 604 source : AE3 104) chain E residue 534 type sequence T description binding site for residue GOL E 604 source : AE3 105) chain E residue 85 type sequence R description binding site for residue GOL E 605 source : AE4 106) chain E residue 282 type sequence K description binding site for residue GOL E 605 source : AE4 107) chain E residue 305 type sequence A description binding site for residue GOL E 605 source : AE4 108) chain E residue 307 type sequence G description binding site for residue GOL E 605 source : AE4 109) chain E residue 308 type sequence D description binding site for residue GOL E 605 source : AE4 110) chain E residue 340 type sequence T description binding site for residue GOL E 605 source : AE4 111) chain D residue 421 type sequence T description binding site for residue FLC D 601 source : AE5 112) chain D residue 444 type sequence T description binding site for residue FLC D 601 source : AE5 113) chain D residue 445 type sequence T description binding site for residue FLC D 601 source : AE5 114) chain D residue 446 type sequence T description binding site for residue FLC D 601 source : AE5 115) chain D residue 448 type sequence R description binding site for residue FLC D 601 source : AE5 116) chain D residue 449 type sequence S description binding site for residue FLC D 601 source : AE5 117) chain D residue 69 type sequence S description binding site for residue EDO D 602 source : AE6 118) chain D residue 72 type sequence R description binding site for residue EDO D 602 source : AE6 119) chain E residue 142 type sequence S description binding site for residue EDO D 602 source : AE6 120) chain E residue 143 type sequence E description binding site for residue EDO D 602 source : AE6 121) chain E residue 144 type sequence V description binding site for residue EDO D 602 source : AE6 122) chain D residue 85 type sequence R description binding site for residue GOL D 603 source : AE7 123) chain D residue 284 type sequence E description binding site for residue GOL D 603 source : AE7 124) chain D residue 305 type sequence A description binding site for residue GOL D 603 source : AE7 125) chain D residue 308 type sequence D description binding site for residue GOL D 603 source : AE7 126) chain F residue 333 type sequence G description binding site for residue EDO F 601 source : AE8 127) chain F residue 334 type sequence K description binding site for residue EDO F 601 source : AE8 128) chain F residue 335 type sequence P description binding site for residue EDO F 601 source : AE8 129) chain F residue 369 type sequence D description binding site for residue EDO F 601 source : AE8 130) chain F residue 454 type sequence S description binding site for residue EDO F 601 source : AE8 131) chain F residue 455 type sequence R description binding site for residue EDO F 601 source : AE8 132) chain F residue 457 type sequence R description binding site for residue EDO F 601 source : AE8 133) chain F residue 478 type sequence C description binding site for residue EDO F 601 source : AE8 134) chain F residue 85 type sequence R description binding site for residue GOL F 602 source : AE9 135) chain F residue 282 type sequence K description binding site for residue GOL F 602 source : AE9 136) chain F residue 305 type sequence A description binding site for residue GOL F 602 source : AE9 137) chain F residue 307 type sequence G description binding site for residue GOL F 602 source : AE9 138) chain F residue 308 type sequence D description binding site for residue GOL F 602 source : AE9 139) chain F residue 340 type sequence T description binding site for residue GOL F 602 source : AE9 140) chain F residue 444 type sequence T description binding site for residue GOL F 603 source : AF1 141) chain F residue 445 type sequence T description binding site for residue GOL F 603 source : AF1 142) chain F residue 446 type sequence T description binding site for residue GOL F 603 source : AF1 143) chain F residue 448 type sequence R description binding site for residue GOL F 603 source : AF1 144) chain F residue 534 type sequence T description binding site for residue GOL F 603 source : AF1 145) chain G residue 85 type sequence R description binding site for residue EDO G 601 source : AF2 146) chain G residue 305 type sequence A description binding site for residue EDO G 601 source : AF2 147) chain G residue 307 type sequence G description binding site for residue EDO G 601 source : AF2 148) chain G residue 308 type sequence D description binding site for residue EDO G 601 source : AF2 149) chain G residue 340 type sequence T description binding site for residue EDO G 601 source : AF2 150) chain G residue 333 type sequence G description binding site for residue EDO G 602 source : AF3 151) chain G residue 334 type sequence K description binding site for residue EDO G 602 source : AF3 152) chain G residue 335 type sequence P description binding site for residue EDO G 602 source : AF3 153) chain G residue 369 type sequence D description binding site for residue EDO G 602 source : AF3 154) chain G residue 454 type sequence S description binding site for residue EDO G 602 source : AF3 155) chain G residue 455 type sequence R description binding site for residue EDO G 602 source : AF3 156) chain G residue 457 type sequence R description binding site for residue EDO G 602 source : AF3 157) chain G residue 478 type sequence C description binding site for residue EDO G 602 source : AF3 158) chain G residue 444 type sequence T description binding site for residue GOL G 603 source : AF4 159) chain G residue 445 type sequence T description binding site for residue GOL G 603 source : AF4 160) chain G residue 446 type sequence T description binding site for residue GOL G 603 source : AF4 161) chain G residue 448 type sequence R description binding site for residue GOL G 603 source : AF4 162) chain G residue 449 type sequence S description binding site for residue GOL G 603 source : AF4 163) chain H residue 85 type sequence R description binding site for residue GOL H 601 source : AF5 164) chain H residue 282 type sequence K description binding site for residue GOL H 601 source : AF5 165) chain H residue 284 type sequence E description binding site for residue GOL H 601 source : AF5 166) chain H residue 305 type sequence A description binding site for residue GOL H 601 source : AF5 167) chain H residue 307 type sequence G description binding site for residue GOL H 601 source : AF5 168) chain H residue 308 type sequence D description binding site for residue GOL H 601 source : AF5 169) chain H residue 340 type sequence T description binding site for residue GOL H 601 source : AF5 170) chain H residue 444 type sequence T description binding site for residue GOL H 602 source : AF6 171) chain H residue 445 type sequence T description binding site for residue GOL H 602 source : AF6 172) chain H residue 446 type sequence T description binding site for residue GOL H 602 source : AF6 173) chain H residue 449 type sequence S description binding site for residue GOL H 602 source : AF6 174) chain A residue 277-289 type prosite sequence IKIISKIENHEGV description PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV source prosite : PS00110 175) chain D residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 176) chain F residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 177) chain F residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 178) chain G residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 179) chain G residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 180) chain H residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 181) chain H residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 182) chain D residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 183) chain B residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 184) chain C residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 185) chain C residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 186) chain E residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 187) chain E residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 188) chain A residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 189) chain A residue 89 type BINDING sequence S description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 190) chain B residue 85 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGB source Swiss-Prot : SWS_FT_FI1 191) chain B residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 192) chain B residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 193) chain B residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 194) chain B residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 195) chain B residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 196) chain B residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 197) chain B residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 198) chain C residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 199) chain C residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 200) chain C residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 201) chain C residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 202) chain C residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 203) chain C residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 204) chain C residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 205) chain C residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 206) chain C residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 207) chain C residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 208) chain C residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 209) chain C residue 528 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 210) chain E residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 211) chain E residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 212) chain E residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 213) chain E residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 214) chain E residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 215) chain E residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 216) chain E residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 217) chain E residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 218) chain E residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 219) chain E residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 220) chain E residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 221) chain E residue 528 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 222) chain D residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 223) chain D residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 224) chain D residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 225) chain D residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 226) chain D residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 227) chain D residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 228) chain D residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 229) chain D residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 230) chain D residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 231) chain D residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 232) chain D residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 233) chain D residue 528 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 234) chain F residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 235) chain F residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 236) chain F residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 237) chain F residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 238) chain F residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 239) chain F residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 240) chain F residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 241) chain F residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 242) chain F residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 243) chain F residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 244) chain F residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 245) chain G residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 246) chain G residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 247) chain G residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 248) chain G residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 249) chain G residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 250) chain G residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 251) chain G residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 252) chain G residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 253) chain G residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 254) chain G residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 255) chain G residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 256) chain H residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 257) chain H residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 258) chain H residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 259) chain H residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 260) chain H residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 261) chain H residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 262) chain H residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 263) chain H residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 264) chain H residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 265) chain H residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 266) chain A residue 494 type BINDING sequence W description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 267) chain A residue 501 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 268) chain B residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 269) chain B residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 270) chain B residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 271) chain B residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 272) chain A residue 284 type BINDING sequence E description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 273) chain A residue 307 type BINDING sequence G description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 274) chain A residue 308 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 275) chain A residue 340 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 276) chain A residue 444 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 277) chain A residue 87 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 278) chain A residue 125 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 279) chain A residue 126 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 280) chain A residue 282 type BINDING sequence K description BINDING => ECO:0000269|PubMed:11960989, ECO:0007744|PDB:2VGF source Swiss-Prot : SWS_FT_FI2 281) chain B residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 282) chain D residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 283) chain G residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 284) chain G residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 285) chain D residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 286) chain C residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 287) chain C residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 288) chain E residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 289) chain E residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 290) chain A residue 132 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 291) chain A residue 219 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14618 source Swiss-Prot : SWS_FT_FI3 292) chain C residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 293) chain E residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 294) chain D residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 295) chain F residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 296) chain G residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 297) chain H residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 298) chain A residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 299) chain B residue 282 type SITE sequence K description Transition state stabilizer => ECO:0000250|UniProtKB:P00549 source Swiss-Prot : SWS_FT_FI4 300) chain D residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 301) chain F residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 302) chain G residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 303) chain H residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 304) chain C residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 305) chain E residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 306) chain A residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 307) chain B residue 261 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5

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