eF-site ID 5q06-C PDB Code 5q06 Chain C 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-(2-methyl-1,3-thiazol-4-yl)phenyl]sulfonylurea Classification HYDROLASE/HYDROLASE INHIBITOR Compound Fructose-1,6-bisphosphatase 1 Source (Q2TU34_HUMAN) Sequence C:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKKLDVLSNDLVMNMLKSSFATCVLVSE EDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFG IYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAM DCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAK DFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLV YGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATT GKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS Description Functional site 1) chain C residue 16 type sequence F description binding site for residue 95V C 401 source : AC3 2) chain C residue 18 type sequence M description binding site for residue 95V C 401 source : AC3 3) chain C residue 20 type sequence E description binding site for residue 95V C 401 source : AC3 4) chain C residue 21 type sequence G description binding site for residue 95V C 401 source : AC3 5) chain C residue 22 type sequence R description binding site for residue 95V C 401 source : AC3 6) chain C residue 24 type sequence A description binding site for residue 95V C 401 source : AC3 7) chain C residue 26 type sequence G description binding site for residue 95V C 401 source : AC3 8) chain C residue 27 type sequence T description binding site for residue 95V C 401 source : AC3 9) chain C residue 28 type sequence G description binding site for residue 95V C 401 source : AC3 10) chain C residue 29 type sequence E description binding site for residue 95V C 401 source : AC3 11) chain C residue 30 type sequence L description binding site for residue 95V C 401 source : AC3 12) chain C residue 31 type sequence T description binding site for residue 95V C 401 source : AC3 13) chain C residue 177 type sequence M description binding site for residue 95V C 401 source : AC3 14) chain C residue 179 type sequence C description binding site for residue 95V C 401 source : AC3 15) chain C residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 16) chain C residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 17) chain C residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 18) chain C residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 19) chain C residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 20) chain C residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 21) chain C residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 22) chain C residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 23) chain C residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 24) chain C residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 25) chain C residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 26) chain C residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 27) chain C residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 28) chain C residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 29) chain C residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 30) chain C residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 31) chain C residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7

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