eF-site ID 5q06-B PDB Code 5q06 Chain B 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 B:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS Description Functional site 1) chain B residue 16 type sequence F description binding site for residue 95V B 401 source : AC2 2) chain B residue 20 type sequence E description binding site for residue 95V B 401 source : AC2 3) chain B residue 21 type sequence G description binding site for residue 95V B 401 source : AC2 4) chain B residue 22 type sequence R description binding site for residue 95V B 401 source : AC2 5) chain B residue 26 type sequence G description binding site for residue 95V B 401 source : AC2 6) chain B residue 27 type sequence T description binding site for residue 95V B 401 source : AC2 7) chain B residue 28 type sequence G description binding site for residue 95V B 401 source : AC2 8) chain B residue 29 type sequence E description binding site for residue 95V B 401 source : AC2 9) chain B residue 30 type sequence L description binding site for residue 95V B 401 source : AC2 10) chain B residue 31 type sequence T description binding site for residue 95V B 401 source : AC2 11) chain B residue 177 type sequence M description binding site for residue 95V B 401 source : AC2 12) chain B residue 179 type sequence C description binding site for residue 95V B 401 source : AC2 13) chain B residue 27 type sequence T description binding site for residue 95V D 401 source : AC4 14) chain B residue 28 type sequence G description binding site for residue 95V D 401 source : AC4 15) chain B residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 16) chain B residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 17) chain B residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 18) chain B residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 19) chain B residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 20) chain B residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 26) chain B residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 27) chain B residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 28) chain B residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 29) chain B residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 30) chain B residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 31) chain B residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7

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