eF-site ID 5pzw-ABCD PDB Code 5pzw 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-(3-chlorophenyl)sulfonyl-3-[5-[(3-chlorophenyl)sulfonylcarbamoylamino]pentyl]urea 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 94J A 401 source : AC1 2) chain A residue 18 type sequence M description binding site for residue 94J A 401 source : AC1 3) chain A residue 21 type sequence G description binding site for residue 94J A 401 source : AC1 4) chain A residue 24 type sequence A description binding site for residue 94J A 401 source : AC1 5) chain A residue 26 type sequence G description binding site for residue 94J A 401 source : AC1 6) chain A residue 27 type sequence T description binding site for residue 94J A 401 source : AC1 7) chain A residue 28 type sequence G description binding site for residue 94J A 401 source : AC1 8) chain A residue 29 type sequence E description binding site for residue 94J A 401 source : AC1 9) chain A residue 30 type sequence L description binding site for residue 94J A 401 source : AC1 10) chain A residue 31 type sequence T description binding site for residue 94J A 401 source : AC1 11) chain C residue 17 type sequence V description binding site for residue 94J A 401 source : AC1 12) chain C residue 18 type sequence M description binding site for residue 94J A 401 source : AC1 13) chain C residue 21 type sequence G description binding site for residue 94J A 401 source : AC1 14) chain C residue 24 type sequence A description binding site for residue 94J A 401 source : AC1 15) chain C residue 26 type sequence G description binding site for residue 94J A 401 source : AC1 16) chain C residue 27 type sequence T description binding site for residue 94J A 401 source : AC1 17) chain C residue 28 type sequence G description binding site for residue 94J A 401 source : AC1 18) chain C residue 29 type sequence E description binding site for residue 94J A 401 source : AC1 19) chain C residue 30 type sequence L description binding site for residue 94J A 401 source : AC1 20) chain C residue 31 type sequence T description binding site for residue 94J A 401 source : AC1 21) chain A residue 17 type sequence V description binding site for residue AMZ A 402 source : AC2 22) chain A residue 20 type sequence E description binding site for residue AMZ A 402 source : AC2 23) chain A residue 27 type sequence T description binding site for residue AMZ A 402 source : AC2 24) chain A residue 29 type sequence E description binding site for residue AMZ A 402 source : AC2 25) chain A residue 30 type sequence L description binding site for residue AMZ A 402 source : AC2 26) chain A residue 31 type sequence T description binding site for residue AMZ A 402 source : AC2 27) chain A residue 112 type sequence K description binding site for residue AMZ A 402 source : AC2 28) chain A residue 113 type sequence Y description binding site for residue AMZ A 402 source : AC2 29) chain A residue 140 type sequence R description binding site for residue AMZ A 402 source : AC2 30) chain C residue 17 type sequence V description binding site for residue AMZ A 402 source : AC2 31) chain C residue 20 type sequence E description binding site for residue AMZ A 402 source : AC2 32) chain C residue 21 type sequence G description binding site for residue AMZ A 402 source : AC2 33) chain C residue 26 type sequence G description binding site for residue AMZ A 402 source : AC2 34) chain C residue 27 type sequence T description binding site for residue AMZ A 402 source : AC2 35) chain C residue 28 type sequence G description binding site for residue AMZ A 402 source : AC2 36) chain C residue 29 type sequence E description binding site for residue AMZ A 402 source : AC2 37) chain C residue 30 type sequence L description binding site for residue AMZ A 402 source : AC2 38) chain C residue 31 type sequence T description binding site for residue AMZ A 402 source : AC2 39) chain C residue 112 type sequence K description binding site for residue AMZ A 402 source : AC2 40) chain C residue 113 type sequence Y description binding site for residue AMZ A 402 source : AC2 41) chain C residue 160 type sequence V description binding site for residue AMZ A 402 source : AC2 42) chain C residue 177 type sequence M description binding site for residue AMZ A 402 source : AC2 43) chain B residue 17 type sequence V description binding site for residue 94J B 401 source : AC3 44) chain B residue 18 type sequence M description binding site for residue 94J B 401 source : AC3 45) chain B residue 21 type sequence G description binding site for residue 94J B 401 source : AC3 46) chain B residue 22 type sequence R description binding site for residue 94J B 401 source : AC3 47) chain B residue 24 type sequence A description binding site for residue 94J B 401 source : AC3 48) chain B residue 26 type sequence G description binding site for residue 94J B 401 source : AC3 49) chain B residue 27 type sequence T description binding site for residue 94J B 401 source : AC3 50) chain B residue 28 type sequence G description binding site for residue 94J B 401 source : AC3 51) chain B residue 29 type sequence E description binding site for residue 94J B 401 source : AC3 52) chain B residue 30 type sequence L description binding site for residue 94J B 401 source : AC3 53) chain B residue 31 type sequence T description binding site for residue 94J B 401 source : AC3 54) chain D residue 17 type sequence V description binding site for residue 94J B 401 source : AC3 55) chain D residue 18 type sequence M description binding site for residue 94J B 401 source : AC3 56) chain D residue 21 type sequence G description binding site for residue 94J B 401 source : AC3 57) chain D residue 22 type sequence R description binding site for residue 94J B 401 source : AC3 58) chain D residue 24 type sequence A description binding site for residue 94J B 401 source : AC3 59) chain D residue 26 type sequence G description binding site for residue 94J B 401 source : AC3 60) chain D residue 27 type sequence T description binding site for residue 94J B 401 source : AC3 61) chain D residue 28 type sequence G description binding site for residue 94J B 401 source : AC3 62) chain D residue 29 type sequence E description binding site for residue 94J B 401 source : AC3 63) chain D residue 30 type sequence L description binding site for residue 94J B 401 source : AC3 64) chain D residue 31 type sequence T description binding site for residue 94J B 401 source : AC3 65) chain B residue 17 type sequence V description binding site for residue AMZ D 401 source : AC4 66) chain B residue 20 type sequence E description binding site for residue AMZ D 401 source : AC4 67) chain B residue 21 type sequence G description binding site for residue AMZ D 401 source : AC4 68) chain B residue 27 type sequence T description binding site for residue AMZ D 401 source : AC4 69) chain B residue 28 type sequence G description binding site for residue AMZ D 401 source : AC4 70) chain B residue 29 type sequence E description binding site for residue AMZ D 401 source : AC4 71) chain B residue 30 type sequence L description binding site for residue AMZ D 401 source : AC4 72) chain B residue 31 type sequence T description binding site for residue AMZ D 401 source : AC4 73) chain B residue 112 type sequence K description binding site for residue AMZ D 401 source : AC4 74) chain B residue 113 type sequence Y description binding site for residue AMZ D 401 source : AC4 75) chain B residue 140 type sequence R description binding site for residue AMZ D 401 source : AC4 76) chain D residue 17 type sequence V description binding site for residue AMZ D 401 source : AC4 77) chain D residue 20 type sequence E description binding site for residue AMZ D 401 source : AC4 78) chain D residue 21 type sequence G description binding site for residue AMZ D 401 source : AC4 79) chain D residue 27 type sequence T description binding site for residue AMZ D 401 source : AC4 80) chain D residue 28 type sequence G description binding site for residue AMZ D 401 source : AC4 81) chain D residue 29 type sequence E description binding site for residue AMZ D 401 source : AC4 82) chain D residue 30 type sequence L description binding site for residue AMZ D 401 source : AC4 83) chain D residue 31 type sequence T description binding site for residue AMZ D 401 source : AC4 84) chain D residue 112 type sequence K description binding site for residue AMZ D 401 source : AC4 85) chain D residue 113 type sequence Y description binding site for residue AMZ D 401 source : AC4 86) chain D residue 140 type sequence R description binding site for residue AMZ D 401 source : AC4 87) chain A residue 273-285 type prosite sequence GKLRLLYECNPMA description FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA source prosite : PS00124 88) chain A residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 89) chain C residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 90) chain C residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 91) chain C residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 92) chain D residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 93) chain D residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 94) chain D residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 95) chain D residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 96) chain A residue 27 type BINDING sequence T 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 A residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 99) chain B residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 100) chain B residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 101) chain B residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 102) chain B residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 103) chain C residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 104) chain B residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 105) chain B residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 106) chain B residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 107) chain B residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 108) chain B residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 109) chain C residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 110) chain C residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 111) chain C residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 112) chain C residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 113) chain A residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 114) chain C residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 115) chain C residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 116) chain D residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 117) chain D residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 118) chain D residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 119) chain D residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 120) chain D residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 121) chain D residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 122) chain A residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 123) chain A residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 124) chain A residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 125) chain A residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 126) chain A residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 127) chain B residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 128) chain A residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 129) chain D residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 130) chain D residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 131) chain D residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 132) chain A residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 133) chain A residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 134) chain B residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 135) chain B residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 136) chain B residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 137) chain C residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 138) chain C residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 139) chain C residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 140) chain A residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 141) chain B residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 142) chain C residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 143) chain D residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 144) chain A residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 145) chain A residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 146) chain B residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 147) chain B residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 148) chain C residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 149) chain C residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 150) chain D residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 151) chain D residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 152) chain A residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 153) chain B residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 154) chain C residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 155) 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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