eF-site ID 5pzy-G PDB Code 5pzy Chain G 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-(2-chlorophenyl)sulfonylurea Classification HYDROLASE/HYDROLASE INHIBITOR Compound Fructose-1,6-bisphosphatase 1 Source (Q2TU34_HUMAN) Sequence G:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS Description Functional site 1) chain G residue 27 type sequence T description binding site for residue 94V E 401 source : AC5 2) chain G residue 17 type sequence V description binding site for residue 94V G 401 source : AC7 3) chain G residue 18 type sequence M description binding site for residue 94V G 401 source : AC7 4) chain G residue 21 type sequence G description binding site for residue 94V G 401 source : AC7 5) chain G residue 22 type sequence R description binding site for residue 94V G 401 source : AC7 6) chain G residue 24 type sequence A description binding site for residue 94V G 401 source : AC7 7) chain G residue 26 type sequence G description binding site for residue 94V G 401 source : AC7 8) chain G residue 27 type sequence T description binding site for residue 94V G 401 source : AC7 9) chain G residue 28 type sequence G description binding site for residue 94V G 401 source : AC7 10) chain G residue 29 type sequence E description binding site for residue 94V G 401 source : AC7 11) chain G residue 30 type sequence L description binding site for residue 94V G 401 source : AC7 12) chain G residue 31 type sequence T description binding site for residue 94V G 401 source : AC7 13) chain G residue 17 type BINDING sequence V description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 14) chain G residue 27 type BINDING sequence T description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 15) chain G residue 112 type BINDING sequence K description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 16) chain G residue 140 type BINDING sequence R description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA source Swiss-Prot : SWS_FT_FI1 17) chain G residue 97 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 18) chain G residue 120 type BINDING sequence L description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 19) chain G residue 212 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 20) chain G residue 243 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 21) chain G residue 264 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 22) chain G residue 274 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P00636 source Swiss-Prot : SWS_FT_FI2 23) chain G residue 118 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 24) chain G residue 121 type BINDING sequence D description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 25) chain G residue 280 type BINDING sequence E description BINDING => ECO:0007744|PDB:2FHY source Swiss-Prot : SWS_FT_FI3 26) chain G residue 150 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI5 27) chain G residue 215 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 28) chain G residue 244 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6 source Swiss-Prot : SWS_FT_FI6 29) chain G residue 264 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links