eF-site ID 5q01-H PDB Code 5q01 Chain 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-[4-(4,5-dichloro-2-methylpyrazol-3-yl)oxyphenyl]sulfonylurea Classification HYDROLASE/HYDROLASE INHIBITOR Compound Fructose-1,6-bisphosphatase 1 Source (Q2TU34_HUMAN) Sequence H:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS Description Functional site 1) chain H residue 27 type sequence T description binding site for residue 95G F 401 source : AC6 2) chain H residue 28 type sequence G description binding site for residue 95G F 401 source : AC6 3) chain H residue 17 type sequence V description binding site for residue 95G H 401 source : AC8 4) chain H residue 20 type sequence E description binding site for residue 95G H 401 source : AC8 5) chain H residue 21 type sequence G description binding site for residue 95G H 401 source : AC8 6) chain H residue 22 type sequence R description binding site for residue 95G H 401 source : AC8 7) chain H residue 26 type sequence G description binding site for residue 95G H 401 source : AC8 8) chain H residue 27 type sequence T description binding site for residue 95G H 401 source : AC8 9) chain H residue 28 type sequence G description binding site for residue 95G H 401 source : AC8 10) chain H residue 29 type sequence E description binding site for residue 95G H 401 source : AC8 11) chain H residue 30 type sequence L description binding site for residue 95G H 401 source : AC8 12) chain H residue 31 type sequence T description binding site for residue 95G H 401 source : AC8 13) chain H residue 161 type sequence A description binding site for residue 95G H 401 source : AC8 14) chain H residue 175 type sequence L description binding site for residue 95G H 401 source : AC8 15) chain H residue 177 type sequence M description binding site for residue 95G H 401 source : AC8 16) chain H residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 17) chain H residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 18) chain H residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 19) chain H residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7 20) chain H residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 21) chain H residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 22) chain H residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 23) chain H residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 24) chain H residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 25) chain H residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 26) chain H residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 27) chain H residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 28) chain H residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 29) chain H residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 30) chain H residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 31) chain H residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 32) chain H residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3

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