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