eF-site ID 5pzw-D PDB Code 5pzw Chain 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 D:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS Description Functional site 1) chain D residue 17 type sequence V description binding site for residue 94J B 401 source : AC3 2) chain D residue 18 type sequence M description binding site for residue 94J B 401 source : AC3 3) chain D residue 21 type sequence G description binding site for residue 94J B 401 source : AC3 4) chain D residue 22 type sequence R description binding site for residue 94J B 401 source : AC3 5) chain D residue 24 type sequence A description binding site for residue 94J B 401 source : AC3 6) chain D residue 26 type sequence G description binding site for residue 94J B 401 source : AC3 7) chain D residue 27 type sequence T description binding site for residue 94J B 401 source : AC3 8) chain D residue 28 type sequence G description binding site for residue 94J B 401 source : AC3 9) chain D residue 29 type sequence E description binding site for residue 94J B 401 source : AC3 10) chain D residue 30 type sequence L description binding site for residue 94J B 401 source : AC3 11) chain D residue 31 type sequence T description binding site for residue 94J B 401 source : AC3 12) chain D residue 17 type sequence V description binding site for residue AMZ D 401 source : AC4 13) chain D residue 20 type sequence E description binding site for residue AMZ D 401 source : AC4 14) chain D residue 21 type sequence G description binding site for residue AMZ D 401 source : AC4 15) chain D residue 27 type sequence T description binding site for residue AMZ D 401 source : AC4 16) chain D residue 28 type sequence G description binding site for residue AMZ D 401 source : AC4 17) chain D residue 29 type sequence E description binding site for residue AMZ D 401 source : AC4 18) chain D residue 30 type sequence L description binding site for residue AMZ D 401 source : AC4 19) chain D residue 31 type sequence T description binding site for residue AMZ D 401 source : AC4 20) chain D residue 112 type sequence K description binding site for residue AMZ D 401 source : AC4 21) chain D residue 113 type sequence Y description binding site for residue AMZ D 401 source : AC4 22) chain D residue 140 type sequence R description binding site for residue AMZ D 401 source : AC4 23) chain D residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 24) chain D residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 25) chain D residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 26) chain D residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 27) chain D residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 28) chain D residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 29) chain D residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 30) chain D residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 31) chain D residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 32) chain D residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 33) chain D residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 34) chain D residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 35) chain D residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 36) chain D residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 37) chain D residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 38) chain D residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 39) chain D residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5

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