eF-site ID 5q03-ABCDEFGH PDB Code 5q03 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-(5-bromo-1,3-thiazol-2-yl)-3-[5-(2-methylpropyl)thiophen-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 21 type sequence G description binding site for residue 95M A 401 source : AC1 2) chain A residue 22 type sequence R description binding site for residue 95M A 401 source : AC1 3) chain A residue 26 type sequence G description binding site for residue 95M A 401 source : AC1 4) chain A residue 27 type sequence T description binding site for residue 95M A 401 source : AC1 5) chain A residue 28 type sequence G description binding site for residue 95M A 401 source : AC1 6) chain A residue 30 type sequence L description binding site for residue 95M A 401 source : AC1 7) chain A residue 31 type sequence T description binding site for residue 95M A 401 source : AC1 8) chain A residue 177 type sequence M description binding site for residue 95M A 401 source : AC1 9) chain B residue 21 type sequence G description binding site for residue 95M B 401 source : AC2 10) chain B residue 22 type sequence R description binding site for residue 95M B 401 source : AC2 11) chain B residue 24 type sequence A description binding site for residue 95M B 401 source : AC2 12) chain B residue 26 type sequence G description binding site for residue 95M B 401 source : AC2 13) chain B residue 27 type sequence T description binding site for residue 95M B 401 source : AC2 14) chain B residue 28 type sequence G description binding site for residue 95M B 401 source : AC2 15) chain B residue 30 type sequence L description binding site for residue 95M B 401 source : AC2 16) chain B residue 31 type sequence T description binding site for residue 95M B 401 source : AC2 17) chain B residue 177 type sequence M description binding site for residue 95M B 401 source : AC2 18) chain C residue 18 type sequence M description binding site for residue 95M C 401 source : AC3 19) chain C residue 20 type sequence E description binding site for residue 95M C 401 source : AC3 20) chain C residue 21 type sequence G description binding site for residue 95M C 401 source : AC3 21) chain C residue 22 type sequence R description binding site for residue 95M C 401 source : AC3 22) chain C residue 26 type sequence G description binding site for residue 95M C 401 source : AC3 23) chain C residue 27 type sequence T description binding site for residue 95M C 401 source : AC3 24) chain C residue 28 type sequence G description binding site for residue 95M C 401 source : AC3 25) chain C residue 29 type sequence E description binding site for residue 95M C 401 source : AC3 26) chain C residue 30 type sequence L description binding site for residue 95M C 401 source : AC3 27) chain C residue 31 type sequence T description binding site for residue 95M C 401 source : AC3 28) chain C residue 177 type sequence M description binding site for residue 95M C 401 source : AC3 29) chain B residue 27 type sequence T description binding site for residue 95M D 401 source : AC4 30) chain D residue 20 type sequence E description binding site for residue 95M D 401 source : AC4 31) chain D residue 21 type sequence G description binding site for residue 95M D 401 source : AC4 32) chain D residue 22 type sequence R description binding site for residue 95M D 401 source : AC4 33) chain D residue 26 type sequence G description binding site for residue 95M D 401 source : AC4 34) chain D residue 27 type sequence T description binding site for residue 95M D 401 source : AC4 35) chain D residue 28 type sequence G description binding site for residue 95M D 401 source : AC4 36) chain D residue 30 type sequence L description binding site for residue 95M D 401 source : AC4 37) chain D residue 31 type sequence T description binding site for residue 95M D 401 source : AC4 38) chain D residue 177 type sequence M description binding site for residue 95M D 401 source : AC4 39) chain E residue 18 type sequence M description binding site for residue 95M E 401 source : AC5 40) chain E residue 21 type sequence G description binding site for residue 95M E 401 source : AC5 41) chain E residue 22 type sequence R description binding site for residue 95M E 401 source : AC5 42) chain E residue 26 type sequence G description binding site for residue 95M E 401 source : AC5 43) chain E residue 27 type sequence T description binding site for residue 95M E 401 source : AC5 44) chain E residue 28 type sequence G description binding site for residue 95M E 401 source : AC5 45) chain E residue 30 type sequence L description binding site for residue 95M E 401 source : AC5 46) chain E residue 31 type sequence T description binding site for residue 95M E 401 source : AC5 47) chain E residue 177 type sequence M description binding site for residue 95M E 401 source : AC5 48) chain F residue 18 type sequence M description binding site for residue 95M F 401 source : AC6 49) chain F residue 21 type sequence G description binding site for residue 95M F 401 source : AC6 50) chain F residue 26 type sequence G description binding site for residue 95M F 401 source : AC6 51) chain F residue 27 type sequence T description binding site for residue 95M F 401 source : AC6 52) chain F residue 28 type sequence G description binding site for residue 95M F 401 source : AC6 53) chain F residue 30 type sequence L description binding site for residue 95M F 401 source : AC6 54) chain F residue 31 type sequence T description binding site for residue 95M F 401 source : AC6 55) chain G residue 18 type sequence M description binding site for residue 95M G 401 source : AC7 56) chain G residue 21 type sequence G description binding site for residue 95M G 401 source : AC7 57) chain G residue 22 type sequence R description binding site for residue 95M G 401 source : AC7 58) chain G residue 26 type sequence G description binding site for residue 95M G 401 source : AC7 59) chain G residue 27 type sequence T description binding site for residue 95M G 401 source : AC7 60) chain G residue 28 type sequence G description binding site for residue 95M G 401 source : AC7 61) chain G residue 30 type sequence L description binding site for residue 95M G 401 source : AC7 62) chain G residue 31 type sequence T description binding site for residue 95M G 401 source : AC7 63) chain G residue 177 type sequence M description binding site for residue 95M G 401 source : AC7 64) chain F residue 27 type sequence T description binding site for residue 95M H 401 source : AC8 65) chain H residue 20 type sequence E description binding site for residue 95M H 401 source : AC8 66) chain H residue 21 type sequence G description binding site for residue 95M H 401 source : AC8 67) chain H residue 22 type sequence R description binding site for residue 95M H 401 source : AC8 68) chain H residue 24 type sequence A description binding site for residue 95M H 401 source : AC8 69) chain H residue 26 type sequence G description binding site for residue 95M H 401 source : AC8 70) chain H residue 28 type sequence G description binding site for residue 95M H 401 source : AC8 71) chain H residue 30 type sequence L description binding site for residue 95M H 401 source : AC8 72) chain H residue 31 type sequence T description binding site for residue 95M H 401 source : AC8 73) chain H residue 177 type sequence M description binding site for residue 95M H 401 source : AC8 74) chain A residue 273-285 type prosite sequence GKLRLLYECNPMA description FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA source prosite : PS00124 75) chain A residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 76) chain C residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 77) chain C residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 78) chain C residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 79) chain D residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 80) chain D residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 81) chain D residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 82) chain D residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 83) chain E residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 84) chain E residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 85) chain E residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 86) chain A residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 87) chain E residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 88) chain F residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 89) chain F residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 90) chain F residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 91) chain F residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 92) chain G residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 93) chain G residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 94) chain G residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 95) chain G residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 96) chain H residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 97) chain A residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 98) chain H residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 99) chain H residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 100) chain H residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 101) chain A residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 102) chain B residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 103) chain B residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 104) chain B residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 105) chain B residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 106) chain C residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 107) chain B residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 108) chain B residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 109) chain B residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 110) chain B residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 111) chain B residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 112) chain C residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 113) chain C residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 114) chain C residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 115) chain C residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 116) chain A residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 117) chain C residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 118) chain C residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 119) chain D residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 120) chain D residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 121) chain D residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 122) chain D residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 123) chain D residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 124) chain D residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 125) chain A residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 126) chain E residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 127) chain E residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 128) chain E residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 129) chain E residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 130) chain E residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 131) chain E residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 132) chain F residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 133) chain F residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 134) chain F residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 135) chain A residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 136) chain F residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 137) chain F residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 138) chain F residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 139) chain G residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 140) chain G residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 141) chain G residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 142) chain G residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 143) chain G residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 144) chain G residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 145) chain A residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 146) chain H residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 147) chain H residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 148) chain H residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 149) chain H residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 150) chain H residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 151) chain H residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 152) chain A residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 153) chain A residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 154) chain B residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 155) chain A residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 156) chain D residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 157) chain D residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 158) chain D residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 159) chain E residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 160) chain E residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 161) chain E residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 162) chain F residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 163) chain F residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 164) chain F residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 165) chain G residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 166) chain A residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 167) chain G residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 168) chain G residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 169) chain H residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 170) chain H residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 171) chain H residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 172) chain A residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 173) chain B residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 174) chain B residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 175) chain B residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 176) chain C residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 177) chain C residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 178) chain C residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 179) chain A residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 180) chain B residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 181) chain C residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 182) chain D residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 183) chain E residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 184) chain F residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 185) chain G residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 186) chain H residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 187) chain A residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 188) chain E residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 189) chain F residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 190) chain F residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 191) chain G residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 192) chain G residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 193) chain H residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 194) chain H residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 195) chain A residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 196) chain B residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 197) chain B residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 198) chain C residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 199) chain C residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 200) chain D residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 201) chain D residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 202) chain E residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 203) chain A residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 204) chain B residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 205) chain C residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 206) chain D residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 207) chain E residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 208) chain F residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 209) chain G residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 210) chain H residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7

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