eF-site ID 5z2c-ABCDEFGHI PDB Code 5z2c Chain A, B, C, D, E, F, G, H, I click to enlarge Title Crystal structure of ALPK-1 N-terminal domain in complex with ADP-heptose Classification IMMUNE SYSTEM Compound Alpha-protein kinase 1 Source (ALPK1_HUMAN) Sequence A:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPEKWQYKQAVGPEDKTNLK DVIGAGLQQLLASLRASILARDCAAAAAIVFLVDRFLYGL DVSGKLLQVAKGLHKLQPATPIAPQVVIRQARISVNSGKL LKAEYILSSLISNNGATGTWLYRNESDKVLVQSVCIQIRG QILQKLGMWYEAAELIWASIVGYLALPQPDKKGLSTSLGI LADIFVSMSKNDYEKFKNNPQINLSLLKEFDHHLLSAAEA CKLAAAFSAYTPLFVLTAVNIRGTCLLSYSSSNDCPPELK NLHLCEAKEAFEIGLLTKRDDEPVTGKQELHSFVKAAFGL TTVHRRLHGETGTVHAASQLCKEAMGKLYNFSTSSRSQDR EALSQEVMSVIAQVKEHLQVQSFSNVDDRSYVPESFECRL DKLIL B:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPEKWQYKQAVGPEDKTNLK DVIGAGLQQLLASLRASILARDCAAAAAIVFLVDRFLYGL DVSGKLLQVAKGLHKLQPATPIAPQVVIRQARISVNSGKL LKAEYILSSLISNNGATGTWLYRNESDKVLVQSVCIQIRG QILQKLGMWYEAAELIWASIVGYLALPQPDKKGLSTSLGI LADIFVSMSKNDYEKFKNNPQINLSLLKEFDHHLLSAAEA CKLAAAFSAYTPLFVLTAVNIRGTCLLSYSSSNDCPPELK NLHLCEAKEAFEIGLLTKRDDEPVTGKQELHSFVKAAFGL TTVHRRLHGETGTVHAASQLCKEAMGKLYNFSTSSRSQDR EALSQEVMSVIAQVKEHLQVQSFSNVDDRSYVPESFECRL DKLIL C:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPEKWQLKDVIGAGLQQLLA SLRASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVAKG LHKLQPATPIAPQVVIRQARISVNSGKLLKAEYILSSLIS NNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEA AELIWASIVGYLALPQPDKKGLSTSLGILADIFVSMSKND YEKFKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAYTP LFVLTAVNIRGTCLLSYSSSNDCPPELKNLHLCEAKEAFE IGLLTKPVTGKQELHSFVKAAFGLTTVHRRLHGETGTVHA ASQLCKEAMGKLYNFSTSSRSQDREALSQEVMSVIAQVKE HLQVQSFSNDDRSYVPESFECRLDKLI D:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPEKWQYKLKDVIGAGLQQL LASLRASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVA KGLHKLQPATPIAPQVVIRQARISVNSGKLLKAEYILSSL ISNNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWY EAAELIWASIVGYLALPQPDKKGLSTSLGILADIFVSMSK NDYEKFKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAY TPLFVLTAVNIRGTCLLSYSSSNDCPPELKNLHLCEAKEA FEIGLLTKRDEPVTGKQELHSFVKAAFGLTTVHRRLHGET GTVHAASQLCKEAMGKLYNFSTSSRSQDREALSQEVMSVI AQVKEHLQVQSFSNVDDRSYVPESFECRLDKLIL E:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPEWQYLKDVIGAGLQQLLA SLRASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVAKG LHKLQPATPIAPQVVIRQARISVNSGKLLKAEYILSSLIS NNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEA AELIWASIVGYLALPQPDKKGLSTSLGILADIFVSMSKND YEKFKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAYTP LFVLTAVNIRGTCLLSYSSSNDCPPELKNLHLCEAKEAFE IGLLTKRDDEPVTGKQELHSFVKAAFGLTTVHRRLHGETG TVHAASQLCKEAMGKLYNFSTSSRSQDREALSQEVMSVIA QVKEHLQVQSFSNVDDRSYVPESFECRLDKLIL F:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPEKWQYLKDVIGAGLQQLL ASLRASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVAK GLHKLQPATPIAPQVVIRQARISVNSGKLLKAEYILSSLI SNNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYE AAELIWASIVGYLALPQPDKKGLSTSLGILADIFVSMSKN DYEKFKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAYT PLFVLTAVNIRGTCLLSYSSSNDCPPELKNLHLCEAKEAF EIGLLTKRDDEPVTGKQELHSFVKAAFGLTTVHRRLHGET GTVHAASQLCKEAMGKLYNFSTSSRSQDREALSQEVMSVI AQVKEHLQVQSFSNVDDRSYVPESFECRLDKLI G:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPELKDVIGAGLQQLLASLR ASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVAKGLHK LQPATPIAPQVVIRQARISVNSGKLLKAEYILSSLISNNG ATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEAAEL IWASIVGYLALPQPDKKGLSTSLGILADIFVSMSKNDYEK FKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAYTPLFV LTAVNIRGTCLLSYSSSNDCPPELKNLHLCEAKEAFEIGL LTKRDEPVTGKQELHSFVKAAFGLTTVHRRLHGETGTVHA ASQLCKEAMGKLYNFSTSSRSQDREALSQEVMSVIAQVKE HLQVQSFSNVDDRSYVPESFECRLDKLI H:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPELKDVIGAGLQQLLASLR ASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVAKGLHK LQPATPIAPQVVIRQARISVNSGKLLKAEYILSSLISNNG ATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEAAEL IWASIVGYLALPQPDKKGLSTSLGILADIFVSMSKNDYEK FKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAYTPLFV LTAVNIRGTCLLSYSSSNDCPPELKNLHLCEAKEAFEIGL LTKPVTGKQELHSFVKAAFGLTTVHRRLHGETGTVHAASQ LCKEAMGKLYNFSTSSRSQDREALSQEVMSVIAQVKEHLQ VQSFSNDRSYVPESFECRLDKLI I:  NNQKVVAVLLQECKQVLDQLLLEAPDVSEEDKSEDQRCRA LLPSELRTLIQEAKEMKWPFVPEKWQLKDVIGAGLQQLLA SLRASILARDCAAAAAIVFLVDRFLYGLDVSGKLLQVAKG LHKLQPATPIAPQVVIRQARISVNSGKLLKAEYILSSLIS NNGATGTWLYRNESDKVLVQSVCIQIRGQILQKLGMWYEA AELIWASIVGYLALPQPDKKGLSTSLGILADIFVSMSKND YEKFKNNPQINLSLLKEFDHHLLSAAEACKLAAAFSAYTP LFVLTAVNIRGTCLLSYSSSNDCPPHLCEAKEAFEIGLLT KPVTGKQELHSFVKAAFGLTTVHRRLHGETGTVHAASQLC KEAMGKLYNFSTSSRSQDREALSQEVMSVIAQVKEHLDDR SYVPESFE Description Functional site 1) chain A residue 61 type sequence F description binding site for residue AYU A 501 source : AC1 2) chain A residue 67 type sequence Q description binding site for residue AYU A 501 source : AC1 3) chain A residue 68 type sequence Y description binding site for residue AYU A 501 source : AC1 4) chain A residue 116 type sequence R description binding site for residue AYU A 501 source : AC1 5) chain A residue 146 type sequence Q description binding site for residue AYU A 501 source : AC1 6) chain A residue 150 type sequence R description binding site for residue AYU A 501 source : AC1 7) chain A residue 153 type sequence R description binding site for residue AYU A 501 source : AC1 8) chain A residue 195 type sequence V description binding site for residue AYU A 501 source : AC1 9) chain A residue 198 type sequence Q description binding site for residue AYU A 501 source : AC1 10) chain A residue 224 type sequence Y description binding site for residue AYU A 501 source : AC1 11) chain A residue 231 type sequence D description binding site for residue AYU A 501 source : AC1 12) chain A residue 233 type sequence K description binding site for residue AYU A 501 source : AC1 13) chain A residue 234 type sequence G description binding site for residue AYU A 501 source : AC1 14) chain A residue 236 type sequence S description binding site for residue AYU A 501 source : AC1 15) chain A residue 237 type sequence T description binding site for residue AYU A 501 source : AC1 16) chain A residue 295 type sequence F description binding site for residue AYU A 501 source : AC1 17) chain B residue 61 type sequence F description binding site for residue AYU B 501 source : AC2 18) chain B residue 67 type sequence Q description binding site for residue AYU B 501 source : AC2 19) chain B residue 68 type sequence Y description binding site for residue AYU B 501 source : AC2 20) chain B residue 116 type sequence R description binding site for residue AYU B 501 source : AC2 21) chain B residue 119 type sequence Y description binding site for residue AYU B 501 source : AC2 22) chain B residue 146 type sequence Q description binding site for residue AYU B 501 source : AC2 23) chain B residue 150 type sequence R description binding site for residue AYU B 501 source : AC2 24) chain B residue 153 type sequence R description binding site for residue AYU B 501 source : AC2 25) chain B residue 195 type sequence V description binding site for residue AYU B 501 source : AC2 26) chain B residue 198 type sequence Q description binding site for residue AYU B 501 source : AC2 27) chain B residue 224 type sequence Y description binding site for residue AYU B 501 source : AC2 28) chain B residue 231 type sequence D description binding site for residue AYU B 501 source : AC2 29) chain B residue 233 type sequence K description binding site for residue AYU B 501 source : AC2 30) chain B residue 234 type sequence G description binding site for residue AYU B 501 source : AC2 31) chain B residue 236 type sequence S description binding site for residue AYU B 501 source : AC2 32) chain B residue 237 type sequence T description binding site for residue AYU B 501 source : AC2 33) chain B residue 295 type sequence F description binding site for residue AYU B 501 source : AC2 34) chain C residue 61 type sequence F description binding site for residue AYU C 501 source : AC3 35) chain C residue 67 type sequence Q description binding site for residue AYU C 501 source : AC3 36) chain C residue 116 type sequence R description binding site for residue AYU C 501 source : AC3 37) chain C residue 119 type sequence Y description binding site for residue AYU C 501 source : AC3 38) chain C residue 146 type sequence Q description binding site for residue AYU C 501 source : AC3 39) chain C residue 150 type sequence R description binding site for residue AYU C 501 source : AC3 40) chain C residue 153 type sequence R description binding site for residue AYU C 501 source : AC3 41) chain C residue 195 type sequence V description binding site for residue AYU C 501 source : AC3 42) chain C residue 198 type sequence Q description binding site for residue AYU C 501 source : AC3 43) chain C residue 224 type sequence Y description binding site for residue AYU C 501 source : AC3 44) chain C residue 231 type sequence D description binding site for residue AYU C 501 source : AC3 45) chain C residue 233 type sequence K description binding site for residue AYU C 501 source : AC3 46) chain C residue 234 type sequence G description binding site for residue AYU C 501 source : AC3 47) chain C residue 236 type sequence S description binding site for residue AYU C 501 source : AC3 48) chain C residue 237 type sequence T description binding site for residue AYU C 501 source : AC3 49) chain C residue 295 type sequence F description binding site for residue AYU C 501 source : AC3 50) chain D residue 61 type sequence F description binding site for residue AYU D 501 source : AC4 51) chain D residue 67 type sequence Q description binding site for residue AYU D 501 source : AC4 52) chain D residue 116 type sequence R description binding site for residue AYU D 501 source : AC4 53) chain D residue 119 type sequence Y description binding site for residue AYU D 501 source : AC4 54) chain D residue 146 type sequence Q description binding site for residue AYU D 501 source : AC4 55) chain D residue 150 type sequence R description binding site for residue AYU D 501 source : AC4 56) chain D residue 153 type sequence R description binding site for residue AYU D 501 source : AC4 57) chain D residue 195 type sequence V description binding site for residue AYU D 501 source : AC4 58) chain D residue 198 type sequence Q description binding site for residue AYU D 501 source : AC4 59) chain D residue 224 type sequence Y description binding site for residue AYU D 501 source : AC4 60) chain D residue 231 type sequence D description binding site for residue AYU D 501 source : AC4 61) chain D residue 233 type sequence K description binding site for residue AYU D 501 source : AC4 62) chain D residue 234 type sequence G description binding site for residue AYU D 501 source : AC4 63) chain D residue 236 type sequence S description binding site for residue AYU D 501 source : AC4 64) chain D residue 237 type sequence T description binding site for residue AYU D 501 source : AC4 65) chain D residue 295 type sequence F description binding site for residue AYU D 501 source : AC4 66) chain E residue 61 type sequence F description binding site for residue AYU E 501 source : AC5 67) chain E residue 67 type sequence Q description binding site for residue AYU E 501 source : AC5 68) chain E residue 68 type sequence Y description binding site for residue AYU E 501 source : AC5 69) chain E residue 116 type sequence R description binding site for residue AYU E 501 source : AC5 70) chain E residue 119 type sequence Y description binding site for residue AYU E 501 source : AC5 71) chain E residue 146 type sequence Q description binding site for residue AYU E 501 source : AC5 72) chain E residue 150 type sequence R description binding site for residue AYU E 501 source : AC5 73) chain E residue 153 type sequence R description binding site for residue AYU E 501 source : AC5 74) chain E residue 195 type sequence V description binding site for residue AYU E 501 source : AC5 75) chain E residue 198 type sequence Q description binding site for residue AYU E 501 source : AC5 76) chain E residue 224 type sequence Y description binding site for residue AYU E 501 source : AC5 77) chain E residue 231 type sequence D description binding site for residue AYU E 501 source : AC5 78) chain E residue 233 type sequence K description binding site for residue AYU E 501 source : AC5 79) chain E residue 234 type sequence G description binding site for residue AYU E 501 source : AC5 80) chain E residue 236 type sequence S description binding site for residue AYU E 501 source : AC5 81) chain E residue 237 type sequence T description binding site for residue AYU E 501 source : AC5 82) chain E residue 295 type sequence F description binding site for residue AYU E 501 source : AC5 83) chain F residue 61 type sequence F description binding site for residue AYU F 501 source : AC6 84) chain F residue 67 type sequence Q description binding site for residue AYU F 501 source : AC6 85) chain F residue 68 type sequence Y description binding site for residue AYU F 501 source : AC6 86) chain F residue 116 type sequence R description binding site for residue AYU F 501 source : AC6 87) chain F residue 119 type sequence Y description binding site for residue AYU F 501 source : AC6 88) chain F residue 146 type sequence Q description binding site for residue AYU F 501 source : AC6 89) chain F residue 150 type sequence R description binding site for residue AYU F 501 source : AC6 90) chain F residue 153 type sequence R description binding site for residue AYU F 501 source : AC6 91) chain F residue 195 type sequence V description binding site for residue AYU F 501 source : AC6 92) chain F residue 198 type sequence Q description binding site for residue AYU F 501 source : AC6 93) chain F residue 224 type sequence Y description binding site for residue AYU F 501 source : AC6 94) chain F residue 231 type sequence D description binding site for residue AYU F 501 source : AC6 95) chain F residue 233 type sequence K description binding site for residue AYU F 501 source : AC6 96) chain F residue 234 type sequence G description binding site for residue AYU F 501 source : AC6 97) chain F residue 236 type sequence S description binding site for residue AYU F 501 source : AC6 98) chain F residue 237 type sequence T description binding site for residue AYU F 501 source : AC6 99) chain F residue 295 type sequence F description binding site for residue AYU F 501 source : AC6 100) chain G residue 61 type sequence F description binding site for residue AYU G 501 source : AC7 101) chain G residue 116 type sequence R description binding site for residue AYU G 501 source : AC7 102) chain G residue 119 type sequence Y description binding site for residue AYU G 501 source : AC7 103) chain G residue 146 type sequence Q description binding site for residue AYU G 501 source : AC7 104) chain G residue 150 type sequence R description binding site for residue AYU G 501 source : AC7 105) chain G residue 153 type sequence R description binding site for residue AYU G 501 source : AC7 106) chain G residue 195 type sequence V description binding site for residue AYU G 501 source : AC7 107) chain G residue 198 type sequence Q description binding site for residue AYU G 501 source : AC7 108) chain G residue 224 type sequence Y description binding site for residue AYU G 501 source : AC7 109) chain G residue 231 type sequence D description binding site for residue AYU G 501 source : AC7 110) chain G residue 233 type sequence K description binding site for residue AYU G 501 source : AC7 111) chain G residue 234 type sequence G description binding site for residue AYU G 501 source : AC7 112) chain G residue 236 type sequence S description binding site for residue AYU G 501 source : AC7 113) chain G residue 237 type sequence T description binding site for residue AYU G 501 source : AC7 114) chain G residue 289 type sequence S description binding site for residue AYU G 501 source : AC7 115) chain G residue 295 type sequence F description binding site for residue AYU G 501 source : AC7 116) chain H residue 61 type sequence F description binding site for residue AYU H 501 source : AC8 117) chain H residue 116 type sequence R description binding site for residue AYU H 501 source : AC8 118) chain H residue 119 type sequence Y description binding site for residue AYU H 501 source : AC8 119) chain H residue 146 type sequence Q description binding site for residue AYU H 501 source : AC8 120) chain H residue 149 type sequence I description binding site for residue AYU H 501 source : AC8 121) chain H residue 150 type sequence R description binding site for residue AYU H 501 source : AC8 122) chain H residue 153 type sequence R description binding site for residue AYU H 501 source : AC8 123) chain H residue 195 type sequence V description binding site for residue AYU H 501 source : AC8 124) chain H residue 198 type sequence Q description binding site for residue AYU H 501 source : AC8 125) chain H residue 224 type sequence Y description binding site for residue AYU H 501 source : AC8 126) chain H residue 231 type sequence D description binding site for residue AYU H 501 source : AC8 127) chain H residue 233 type sequence K description binding site for residue AYU H 501 source : AC8 128) chain H residue 234 type sequence G description binding site for residue AYU H 501 source : AC8 129) chain H residue 236 type sequence S description binding site for residue AYU H 501 source : AC8 130) chain H residue 237 type sequence T description binding site for residue AYU H 501 source : AC8 131) chain H residue 295 type sequence F description binding site for residue AYU H 501 source : AC8 132) chain I residue 61 type sequence F description binding site for residue AYU I 501 source : AC9 133) chain I residue 67 type sequence Q description binding site for residue AYU I 501 source : AC9 134) chain I residue 116 type sequence R description binding site for residue AYU I 501 source : AC9 135) chain I residue 119 type sequence Y description binding site for residue AYU I 501 source : AC9 136) chain I residue 146 type sequence Q description binding site for residue AYU I 501 source : AC9 137) chain I residue 150 type sequence R description binding site for residue AYU I 501 source : AC9 138) chain I residue 153 type sequence R description binding site for residue AYU I 501 source : AC9 139) chain I residue 195 type sequence V description binding site for residue AYU I 501 source : AC9 140) chain I residue 224 type sequence Y description binding site for residue AYU I 501 source : AC9 141) chain I residue 231 type sequence D description binding site for residue AYU I 501 source : AC9 142) chain I residue 233 type sequence K description binding site for residue AYU I 501 source : AC9 143) chain I residue 234 type sequence G description binding site for residue AYU I 501 source : AC9 144) chain I residue 236 type sequence S description binding site for residue AYU I 501 source : AC9 145) chain I residue 237 type sequence T description binding site for residue AYU I 501 source : AC9 146) chain I residue 295 type sequence F description binding site for residue AYU I 501 source : AC9 147) chain A residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 148) chain B residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 149) chain B residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 150) chain B residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 151) chain B residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 152) chain B residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 153) chain B residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 154) chain B residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 155) chain C residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 156) chain C residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 157) chain C residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 158) chain A residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 159) chain C residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 160) chain C residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 161) chain C residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 162) chain C residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 163) chain C residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 164) chain D residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 165) chain D residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 166) chain D residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 167) chain D residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 168) chain D residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 169) chain A residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 170) chain D residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 171) chain D residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 172) chain D residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 173) chain E residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 174) chain E residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 175) chain E residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 176) chain E residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 177) chain E residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 178) chain E residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 179) chain E residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 180) chain A residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 181) chain E residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 182) chain F residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 183) chain F residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 184) chain F residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 185) chain F residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 186) chain F residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 187) chain F residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 188) chain F residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 189) chain F residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 190) chain G residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 191) chain A residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 192) chain G residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 193) chain G residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 194) chain G residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 195) chain G residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 196) chain G residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 197) chain G residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 198) chain H residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 199) chain H residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 200) chain A residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 201) chain H residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 202) chain H residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 203) chain H residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 204) chain H residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 205) chain H residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 206) chain I residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 207) chain I residue 67 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 208) chain I residue 116 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 209) chain I residue 150 type BINDING sequence R description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 210) chain I residue 231 type BINDING sequence D description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 211) chain A residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 212) chain I residue 233 type BINDING sequence K description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 213) chain I residue 236 type BINDING sequence S description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 214) chain I residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 215) chain A residue 295 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1 216) chain B residue 61 type BINDING sequence F description BINDING => ECO:0000269|PubMed:30111836 source Swiss-Prot : SWS_FT_FI1

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