eF-site ID 5q02-ABCD PDB Code 5q02 Chain A, B, C, D 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-(1,2-oxazol-3-yl)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 RKAGIAHLYGIAGKKLDVLSNDLVMNMLKSSFATCVLVSE EDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFG IYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAM DCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAK DFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLV YGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATT GKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS D:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS Description Functional site 1) chain A residue 17 type sequence V description binding site for residue 95J A 401 source : AC1 2) chain A residue 18 type sequence M description binding site for residue 95J A 401 source : AC1 3) chain A residue 20 type sequence E description binding site for residue 95J A 401 source : AC1 4) chain A residue 21 type sequence G description binding site for residue 95J A 401 source : AC1 5) chain A residue 22 type sequence R description binding site for residue 95J A 401 source : AC1 6) chain A residue 26 type sequence G description binding site for residue 95J A 401 source : AC1 7) chain A residue 27 type sequence T description binding site for residue 95J A 401 source : AC1 8) chain A residue 28 type sequence G description binding site for residue 95J A 401 source : AC1 9) chain A residue 29 type sequence E description binding site for residue 95J A 401 source : AC1 10) chain A residue 30 type sequence L description binding site for residue 95J A 401 source : AC1 11) chain A residue 31 type sequence T description binding site for residue 95J A 401 source : AC1 12) chain A residue 177 type sequence M description binding site for residue 95J A 401 source : AC1 13) chain A residue 179 type sequence C description binding site for residue 95J A 401 source : AC1 14) chain C residue 27 type sequence T description binding site for residue 95J A 401 source : AC1 15) chain C residue 28 type sequence G description binding site for residue 95J A 401 source : AC1 16) chain B residue 17 type sequence V description binding site for residue 95J B 401 source : AC2 17) chain B residue 18 type sequence M description binding site for residue 95J B 401 source : AC2 18) chain B residue 20 type sequence E description binding site for residue 95J B 401 source : AC2 19) chain B residue 21 type sequence G description binding site for residue 95J B 401 source : AC2 20) chain B residue 22 type sequence R description binding site for residue 95J B 401 source : AC2 21) chain B residue 26 type sequence G description binding site for residue 95J B 401 source : AC2 22) chain B residue 27 type sequence T description binding site for residue 95J B 401 source : AC2 23) chain B residue 28 type sequence G description binding site for residue 95J B 401 source : AC2 24) chain B residue 29 type sequence E description binding site for residue 95J B 401 source : AC2 25) chain B residue 30 type sequence L description binding site for residue 95J B 401 source : AC2 26) chain B residue 31 type sequence T description binding site for residue 95J B 401 source : AC2 27) chain B residue 177 type sequence M description binding site for residue 95J B 401 source : AC2 28) chain B residue 179 type sequence C description binding site for residue 95J B 401 source : AC2 29) chain D residue 27 type sequence T description binding site for residue 95J B 401 source : AC2 30) chain D residue 28 type sequence G description binding site for residue 95J B 401 source : AC2 31) chain A residue 27 type sequence T description binding site for residue 95J C 401 source : AC3 32) chain C residue 18 type sequence M description binding site for residue 95J C 401 source : AC3 33) chain C residue 20 type sequence E description binding site for residue 95J C 401 source : AC3 34) chain C residue 21 type sequence G description binding site for residue 95J C 401 source : AC3 35) chain C residue 22 type sequence R description binding site for residue 95J C 401 source : AC3 36) chain C residue 26 type sequence G description binding site for residue 95J C 401 source : AC3 37) chain C residue 27 type sequence T description binding site for residue 95J C 401 source : AC3 38) chain C residue 28 type sequence G description binding site for residue 95J C 401 source : AC3 39) chain C residue 29 type sequence E description binding site for residue 95J C 401 source : AC3 40) chain C residue 30 type sequence L description binding site for residue 95J C 401 source : AC3 41) chain C residue 31 type sequence T description binding site for residue 95J C 401 source : AC3 42) chain C residue 177 type sequence M description binding site for residue 95J C 401 source : AC3 43) chain C residue 179 type sequence C description binding site for residue 95J C 401 source : AC3 44) chain B residue 27 type sequence T description binding site for residue 95J D 401 source : AC4 45) chain B residue 28 type sequence G description binding site for residue 95J D 401 source : AC4 46) chain D residue 17 type sequence V description binding site for residue 95J D 401 source : AC4 47) chain D residue 18 type sequence M description binding site for residue 95J D 401 source : AC4 48) chain D residue 20 type sequence E description binding site for residue 95J D 401 source : AC4 49) chain D residue 21 type sequence G description binding site for residue 95J D 401 source : AC4 50) chain D residue 22 type sequence R description binding site for residue 95J D 401 source : AC4 51) chain D residue 26 type sequence G description binding site for residue 95J D 401 source : AC4 52) chain D residue 27 type sequence T description binding site for residue 95J D 401 source : AC4 53) chain D residue 28 type sequence G description binding site for residue 95J D 401 source : AC4 54) chain D residue 29 type sequence E description binding site for residue 95J D 401 source : AC4 55) chain D residue 30 type sequence L description binding site for residue 95J D 401 source : AC4 56) chain D residue 31 type sequence T description binding site for residue 95J D 401 source : AC4 57) chain D residue 177 type sequence M description binding site for residue 95J D 401 source : AC4 58) chain A residue 273-285 type prosite sequence GKLRLLYECNPMA description FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA source prosite : PS00124 59) chain A residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 60) chain C residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 61) chain C residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 62) chain C residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 63) chain D residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 64) chain D residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 65) chain D residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 66) chain D residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 67) chain A residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 68) chain A residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 69) chain A residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 70) chain B residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 71) chain B residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 72) chain B residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 73) chain B residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 74) chain C residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 75) chain B residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 76) chain B residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 77) chain B residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 78) chain B residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 79) chain B residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 80) chain C residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 81) chain C residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 82) chain C residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 83) chain C residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 84) chain A residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 85) chain C residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 86) chain C residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 87) chain D residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 88) chain D residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 89) chain D residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 90) chain D residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 91) chain D residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 92) chain D residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 93) chain A residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 94) chain A residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 95) chain A residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 96) chain A residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 97) chain A residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 98) chain B residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 99) chain A residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 100) chain D residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 101) chain D residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 102) chain D residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 103) chain A residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 104) chain A residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 105) chain B residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 106) chain B residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 107) chain B residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 108) chain C residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 109) chain C residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 110) chain C residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 111) chain A residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 112) chain B residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 113) chain C residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 114) chain D residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 115) chain A residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 116) chain A residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 117) chain B residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 118) chain B residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 119) chain C residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 120) chain C residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 121) chain D residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 122) chain D residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 123) chain A residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 124) chain B residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 125) chain C residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 126) chain D residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7

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