eF-site ID 5q07-ABCDEFGH PDB Code 5q07 Chain A, B, C, D, E, F, G, H click to enlarge Title Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(4-bromo-6-morpholin-4-ylpyridin-2-yl)-3-[5-(2-methoxyethyl)-4-methylthiophen-2-yl]sulfonylurea Classification HYDROLASE/HYDROLASE inhibitor Compound Fructose-1,6-bisphosphatase 1 Source (Q2TU34_HUMAN) Sequence A:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGVKKLDVLSNDLVMNMLKSSFATCVLVS EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIF GIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYA KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMAT TGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS B:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS C:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS D:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS E:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGVKKLDVLSNDLVMNMLKSSFATCVLVS EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIF GIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYA KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMAT TGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS F:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS G:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS H:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS Description Functional site 1) chain A residue 17 type sequence V description binding site for residue 95Y A 401 source : AC1 2) chain A residue 21 type sequence G description binding site for residue 95Y A 401 source : AC1 3) chain A residue 22 type sequence R description binding site for residue 95Y A 401 source : AC1 4) chain A residue 24 type sequence A description binding site for residue 95Y A 401 source : AC1 5) chain A residue 25 type sequence R description binding site for residue 95Y A 401 source : AC1 6) chain A residue 26 type sequence G description binding site for residue 95Y A 401 source : AC1 7) chain A residue 27 type sequence T description binding site for residue 95Y A 401 source : AC1 8) chain A residue 28 type sequence G description binding site for residue 95Y A 401 source : AC1 9) chain A residue 29 type sequence E description binding site for residue 95Y A 401 source : AC1 10) chain A residue 30 type sequence L description binding site for residue 95Y A 401 source : AC1 11) chain A residue 31 type sequence T description binding site for residue 95Y A 401 source : AC1 12) chain A residue 160 type sequence V description binding site for residue 95Y A 401 source : AC1 13) chain C residue 26 type sequence G description binding site for residue 95Y A 401 source : AC1 14) chain C residue 27 type sequence T description binding site for residue 95Y A 401 source : AC1 15) chain B residue 17 type sequence V description binding site for residue 95Y B 401 source : AC2 16) chain B residue 20 type sequence E description binding site for residue 95Y B 401 source : AC2 17) chain B residue 21 type sequence G description binding site for residue 95Y B 401 source : AC2 18) chain B residue 22 type sequence R description binding site for residue 95Y B 401 source : AC2 19) chain B residue 24 type sequence A description binding site for residue 95Y B 401 source : AC2 20) chain B residue 25 type sequence R description binding site for residue 95Y B 401 source : AC2 21) chain B residue 26 type sequence G description binding site for residue 95Y B 401 source : AC2 22) chain B residue 27 type sequence T description binding site for residue 95Y B 401 source : AC2 23) chain B residue 28 type sequence G description binding site for residue 95Y B 401 source : AC2 24) chain B residue 29 type sequence E description binding site for residue 95Y B 401 source : AC2 25) chain B residue 30 type sequence L description binding site for residue 95Y B 401 source : AC2 26) chain B residue 31 type sequence T description binding site for residue 95Y B 401 source : AC2 27) chain B residue 160 type sequence V description binding site for residue 95Y B 401 source : AC2 28) chain D residue 26 type sequence G description binding site for residue 95Y B 401 source : AC2 29) chain D residue 27 type sequence T description binding site for residue 95Y B 401 source : AC2 30) chain A residue 26 type sequence G description binding site for residue 95Y C 401 source : AC3 31) chain C residue 17 type sequence V description binding site for residue 95Y C 401 source : AC3 32) chain C residue 21 type sequence G description binding site for residue 95Y C 401 source : AC3 33) chain C residue 22 type sequence R description binding site for residue 95Y C 401 source : AC3 34) chain C residue 24 type sequence A description binding site for residue 95Y C 401 source : AC3 35) chain C residue 26 type sequence G description binding site for residue 95Y C 401 source : AC3 36) chain C residue 28 type sequence G description binding site for residue 95Y C 401 source : AC3 37) chain C residue 29 type sequence E description binding site for residue 95Y C 401 source : AC3 38) chain C residue 30 type sequence L description binding site for residue 95Y C 401 source : AC3 39) chain C residue 31 type sequence T description binding site for residue 95Y C 401 source : AC3 40) chain C residue 177 type sequence M description binding site for residue 95Y C 401 source : AC3 41) chain B residue 26 type sequence G description binding site for residue 95Y D 401 source : AC4 42) chain B residue 27 type sequence T description binding site for residue 95Y D 401 source : AC4 43) chain D residue 17 type sequence V description binding site for residue 95Y D 401 source : AC4 44) chain D residue 21 type sequence G description binding site for residue 95Y D 401 source : AC4 45) chain D residue 22 type sequence R description binding site for residue 95Y D 401 source : AC4 46) chain D residue 24 type sequence A description binding site for residue 95Y D 401 source : AC4 47) chain D residue 25 type sequence R description binding site for residue 95Y D 401 source : AC4 48) chain D residue 26 type sequence G description binding site for residue 95Y D 401 source : AC4 49) chain D residue 27 type sequence T description binding site for residue 95Y D 401 source : AC4 50) chain D residue 28 type sequence G description binding site for residue 95Y D 401 source : AC4 51) chain D residue 30 type sequence L description binding site for residue 95Y D 401 source : AC4 52) chain D residue 31 type sequence T description binding site for residue 95Y D 401 source : AC4 53) chain D residue 177 type sequence M description binding site for residue 95Y D 401 source : AC4 54) chain E residue 17 type sequence V description binding site for residue 95Y E 401 source : AC5 55) chain E residue 21 type sequence G description binding site for residue 95Y E 401 source : AC5 56) chain E residue 22 type sequence R description binding site for residue 95Y E 401 source : AC5 57) chain E residue 25 type sequence R description binding site for residue 95Y E 401 source : AC5 58) chain E residue 26 type sequence G description binding site for residue 95Y E 401 source : AC5 59) chain E residue 27 type sequence T description binding site for residue 95Y E 401 source : AC5 60) chain E residue 28 type sequence G description binding site for residue 95Y E 401 source : AC5 61) chain E residue 29 type sequence E description binding site for residue 95Y E 401 source : AC5 62) chain E residue 30 type sequence L description binding site for residue 95Y E 401 source : AC5 63) chain E residue 31 type sequence T description binding site for residue 95Y E 401 source : AC5 64) chain E residue 160 type sequence V description binding site for residue 95Y E 401 source : AC5 65) chain G residue 27 type sequence T description binding site for residue 95Y E 401 source : AC5 66) chain F residue 21 type sequence G description binding site for residue 95Y F 401 source : AC6 67) chain F residue 22 type sequence R description binding site for residue 95Y F 401 source : AC6 68) chain F residue 26 type sequence G description binding site for residue 95Y F 401 source : AC6 69) chain F residue 27 type sequence T description binding site for residue 95Y F 401 source : AC6 70) chain F residue 28 type sequence G description binding site for residue 95Y F 401 source : AC6 71) chain F residue 30 type sequence L description binding site for residue 95Y F 401 source : AC6 72) chain F residue 31 type sequence T description binding site for residue 95Y F 401 source : AC6 73) chain F residue 160 type sequence V description binding site for residue 95Y F 401 source : AC6 74) chain F residue 177 type sequence M description binding site for residue 95Y F 401 source : AC6 75) chain H residue 26 type sequence G description binding site for residue 95Y F 401 source : AC6 76) chain H residue 27 type sequence T description binding site for residue 95Y F 401 source : AC6 77) chain E residue 26 type sequence G description binding site for residue 95Y G 401 source : AC7 78) chain E residue 27 type sequence T description binding site for residue 95Y G 401 source : AC7 79) chain G residue 21 type sequence G description binding site for residue 95Y G 401 source : AC7 80) chain G residue 22 type sequence R description binding site for residue 95Y G 401 source : AC7 81) chain G residue 25 type sequence R description binding site for residue 95Y G 401 source : AC7 82) chain G residue 26 type sequence G description binding site for residue 95Y G 401 source : AC7 83) chain G residue 27 type sequence T description binding site for residue 95Y G 401 source : AC7 84) chain G residue 28 type sequence G description binding site for residue 95Y G 401 source : AC7 85) chain G residue 29 type sequence E description binding site for residue 95Y G 401 source : AC7 86) chain G residue 30 type sequence L description binding site for residue 95Y G 401 source : AC7 87) chain G residue 31 type sequence T description binding site for residue 95Y G 401 source : AC7 88) chain G residue 160 type sequence V description binding site for residue 95Y G 401 source : AC7 89) chain F residue 26 type sequence G description binding site for residue 95Y H 401 source : AC8 90) chain F residue 27 type sequence T description binding site for residue 95Y H 401 source : AC8 91) chain H residue 17 type sequence V description binding site for residue 95Y H 401 source : AC8 92) chain H residue 20 type sequence E description binding site for residue 95Y H 401 source : AC8 93) chain H residue 21 type sequence G description binding site for residue 95Y H 401 source : AC8 94) chain H residue 22 type sequence R description binding site for residue 95Y H 401 source : AC8 95) chain H residue 25 type sequence R description binding site for residue 95Y H 401 source : AC8 96) chain H residue 26 type sequence G description binding site for residue 95Y H 401 source : AC8 97) chain H residue 28 type sequence G description binding site for residue 95Y H 401 source : AC8 98) chain H residue 29 type sequence E description binding site for residue 95Y H 401 source : AC8 99) chain H residue 30 type sequence L description binding site for residue 95Y H 401 source : AC8 100) chain H residue 31 type sequence T description binding site for residue 95Y H 401 source : AC8 101) chain H residue 160 type sequence V description binding site for residue 95Y H 401 source : AC8 102) chain A residue 273-285 type prosite sequence GKLRLLYECNPMA description FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA source prosite : PS00124 103) chain H residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 104) chain H residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 105) chain H residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 106) chain H residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 107) chain G residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 108) chain G residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 109) chain G residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 110) chain G residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 111) chain B residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 112) chain A residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 113) chain A residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 114) chain A residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 115) chain A residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 116) chain B residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 117) chain B residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 118) chain B residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 119) chain C residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 120) chain C residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 121) chain C residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 122) chain C residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 123) chain D residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 124) chain D residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 125) chain D residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 126) chain D residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 127) chain E residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 128) chain E residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 129) chain E residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 130) chain E residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 131) chain F residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 132) chain F residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 133) chain F residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 134) chain F residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 135) chain H residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 136) chain H residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 137) chain H residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 138) chain H residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 139) chain H residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 140) chain H residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 141) chain C residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 142) chain C residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 143) chain C residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 144) chain C residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 145) chain C residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 146) chain C residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 147) chain D residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 148) chain D residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 149) chain D residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 150) chain D residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 151) chain D residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 152) chain D residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 153) chain E residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 154) chain E residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 155) chain E residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 156) chain E residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 157) chain E residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 158) chain E residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 159) chain F residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 160) chain F residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 161) chain F residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 162) chain F residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 163) chain F residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 164) chain F residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 165) chain G residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 166) chain G residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 167) chain G residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 168) chain G residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 169) chain G residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 170) chain G residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 171) chain B residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 172) chain B residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 173) chain B residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 174) chain B residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 175) chain B residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 176) chain B residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 177) chain A residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 178) chain A residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 179) chain A residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 180) chain A residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 181) chain A residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 182) chain A residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 183) chain H residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 184) chain H residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 185) chain H residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 186) chain D residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 187) chain D residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 188) chain D residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 189) chain E residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 190) chain E residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 191) chain E residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 192) chain F residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 193) chain F residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 194) chain F residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 195) chain G residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 196) chain G residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 197) chain G residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 198) chain C residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 199) chain C residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 200) chain C residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 201) chain A residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 202) chain A residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 203) chain A residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 204) chain B residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 205) chain B residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 206) chain B residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 207) chain H residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 208) chain C residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 209) chain D residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 210) chain E residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 211) chain F residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 212) chain G residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 213) chain A residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 214) chain B residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 215) chain H residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 216) chain H residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 217) chain E residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 218) chain F residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 219) chain F residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 220) chain G residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 221) chain G residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 222) chain C residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 223) chain C residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 224) chain D residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 225) chain D residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 226) chain E residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 227) chain A residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 228) chain A residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 229) chain B residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 230) chain B residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 231) chain H residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 232) chain C residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 233) chain D residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 234) chain E residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 235) chain F residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 236) chain G residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 237) chain A residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 238) chain B residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links