6RJC
E.coli transketolase apoenzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004802 | molecular_function | transketolase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030145 | molecular_function | manganese ion binding |
| A | 0030976 | molecular_function | thiamine pyrophosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004802 | molecular_function | transketolase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030145 | molecular_function | manganese ion binding |
| B | 0030976 | molecular_function | thiamine pyrophosphate binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 701 |
| Chain | Residue |
| A | ASP155 |
| A | ASN185 |
| A | ILE187 |
| A | EDO713 |
| A | EDO714 |
| A | HOH1018 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 702 |
| Chain | Residue |
| A | HOH1289 |
| A | HOH1358 |
| B | ARG483 |
| B | HOH828 |
| A | ILE615 |
| A | ASP617 |
| A | THR633 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 703 |
| Chain | Residue |
| A | TRP307 |
| A | THR326 |
| A | HOH854 |
| A | HOH1256 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 704 |
| Chain | Residue |
| A | LYS131 |
| A | THR172 |
| A | LYS174 |
| A | ASN397 |
| A | HOH1183 |
| A | HOH1228 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 705 |
| Chain | Residue |
| A | TYR620 |
| A | GLY624 |
| A | LEU625 |
| A | ASN626 |
| A | GLY627 |
| A | HOH817 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 706 |
| Chain | Residue |
| A | LEU45 |
| A | HIS47 |
| A | ARG57 |
| A | ASP58 |
| A | PHE60 |
| A | GLU110 |
| A | HOH957 |
| A | HOH1191 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 707 |
| Chain | Residue |
| A | SER559 |
| A | GLU560 |
| A | PHE645 |
| A | HOH849 |
| A | HOH1186 |
| A | HOH1247 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 708 |
| Chain | Residue |
| A | VAL409 |
| A | GLU411 |
| A | PHE437 |
| A | HOH959 |
| B | GLY114 |
| B | PRO115 |
| B | LEU116 |
| B | GLU160 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 709 |
| Chain | Residue |
| A | GLN526 |
| A | GLU527 |
| A | LYS544 |
| A | VAL565 |
| A | HOH1007 |
| A | HOH1310 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 710 |
| Chain | Residue |
| A | GLY114 |
| A | PRO115 |
| A | LEU116 |
| A | GLU160 |
| A | HOH914 |
| B | VAL409 |
| B | GLU411 |
| B | PHE437 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 711 |
| Chain | Residue |
| A | LEU435 |
| A | ASP462 |
| A | PRO475 |
| A | VAL479 |
| A | ARG492 |
| A | GLU612 |
| A | ALA613 |
| A | GLY614 |
| A | HOH1070 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 712 |
| Chain | Residue |
| A | LEU45 |
| A | LYS46 |
| A | HIS47 |
| A | ALA296 |
| A | ALA299 |
| A | LYS303 |
| A | HOH1090 |
| site_id | AD4 |
| Number of Residues | 10 |
| Details | binding site for residue EDO A 713 |
| Chain | Residue |
| A | HIS66 |
| A | GLY154 |
| A | ASP155 |
| A | GLY156 |
| A | ILE187 |
| A | CA701 |
| A | EDO714 |
| A | HOH801 |
| A | HOH1018 |
| B | HOH1477 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 714 |
| Chain | Residue |
| A | HOH804 |
| A | ALA29 |
| A | HIS66 |
| A | ASN185 |
| A | ILE187 |
| A | ILE247 |
| A | HIS261 |
| A | CA701 |
| A | EDO713 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 715 |
| Chain | Residue |
| A | HIS26 |
| A | ILE189 |
| A | HIS261 |
| B | ASP469 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 716 |
| Chain | Residue |
| A | TYR182 |
| A | PHE197 |
| A | THR198 |
| A | ASP199 |
| A | THR201 |
| A | HOH859 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 717 |
| Chain | Residue |
| A | PHE375 |
| A | TRP390 |
| A | SER393 |
| A | ASN403 |
| A | TYR404 |
| A | TYR430 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 718 |
| Chain | Residue |
| A | PHE434 |
| A | HIS461 |
| A | LEU466 |
| A | ASP469 |
| A | HIS473 |
| B | HOH909 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 719 |
| Chain | Residue |
| A | PRO352 |
| A | LYS354 |
| A | ALA524 |
| A | GLN525 |
| B | SER305 |
| B | GLU309 |
| B | HOH831 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 720 |
| Chain | Residue |
| A | ARG42 |
| A | HOH857 |
| A | HOH1141 |
| B | GLY392 |
| B | LYS394 |
| site_id | AE3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 721 |
| Chain | Residue |
| A | SER393 |
| A | LYS394 |
| A | ALA395 |
| A | GLU398 |
| A | HIS406 |
| A | HOH813 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 722 |
| Chain | Residue |
| A | GLU6 |
| A | GLY278 |
| A | TRP279 |
| A | LYS280 |
| A | TYR281 |
| A | HOH812 |
| A | HOH1042 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 723 |
| Chain | Residue |
| A | LYS23 |
| A | HOH805 |
| B | GLU468 |
| B | HOH947 |
| site_id | AE6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 724 |
| Chain | Residue |
| A | ALA292 |
| A | HOH806 |
| A | HOH1099 |
| A | HOH1339 |
| B | ASP399 |
| B | EDO719 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 725 |
| Chain | Residue |
| A | GLY176 |
| A | ALA231 |
| A | VAL234 |
| A | HOH1013 |
| A | HOH1217 |
| site_id | AE8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 726 |
| Chain | Residue |
| A | PRO52 |
| A | SER53 |
| A | GLY108 |
| A | VAL109 |
| A | HOH905 |
| A | HOH917 |
| A | HOH1033 |
| site_id | AE9 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 727 |
| Chain | Residue |
| A | GLN136 |
| A | PHE137 |
| A | ARG139 |
| A | GLU324 |
| A | HOH809 |
| A | HOH839 |
| A | HOH855 |
| A | HOH1105 |
| A | HOH1335 |
| site_id | AF1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 728 |
| Chain | Residue |
| A | LYS342 |
| A | LEU533 |
| A | HOH889 |
| A | HOH1055 |
| site_id | AF2 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 701 |
| Chain | Residue |
| B | ASP155 |
| B | ASN185 |
| B | ILE187 |
| B | HOH939 |
| B | HOH1376 |
| B | HOH1406 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 702 |
| Chain | Residue |
| B | PHE375 |
| B | TRP390 |
| B | SER393 |
| B | ASN403 |
| B | TYR404 |
| B | TYR430 |
| site_id | AF4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 703 |
| Chain | Residue |
| B | ALA271 |
| B | TYR505 |
| B | GLU508 |
| B | ARG509 |
| B | EDO713 |
| B | HOH862 |
| B | HOH946 |
| site_id | AF5 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 704 |
| Chain | Residue |
| B | ARG274 |
| B | GLU275 |
| B | TRP279 |
| B | ARG538 |
| B | GLN592 |
| B | EDO713 |
| B | HOH982 |
| B | HOH1274 |
| B | HOH1479 |
| site_id | AF6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 705 |
| Chain | Residue |
| B | SER559 |
| B | GLU560 |
| B | PHE645 |
| B | PHE650 |
| B | HOH830 |
| B | HOH1068 |
| site_id | AF7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 706 |
| Chain | Residue |
| B | LEU272 |
| B | GLU275 |
| B | ARG509 |
| B | ASP511 |
| B | HOH1109 |
| site_id | AF8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 707 |
| Chain | Residue |
| B | LYS21 |
| B | LYS88 |
| B | GLN92 |
| B | HOH865 |
| B | HOH897 |
| B | HOH1002 |
| site_id | AF9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 708 |
| Chain | Residue |
| B | GLU6 |
| B | GLY278 |
| B | TRP279 |
| B | LYS280 |
| B | TYR281 |
| B | HOH1162 |
| site_id | AG1 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 709 |
| Chain | Residue |
| B | LEU45 |
| B | HIS47 |
| B | ARG57 |
| B | ASP58 |
| B | PHE60 |
| B | GLU110 |
| B | HOH962 |
| B | HOH1102 |
| site_id | AG2 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 710 |
| Chain | Residue |
| B | LYS131 |
| B | THR172 |
| B | LYS174 |
| B | HOH972 |
| B | HOH1061 |
| B | HOH1074 |
| site_id | AG3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 711 |
| Chain | Residue |
| B | THR326 |
| B | EDO718 |
| B | HOH942 |
| site_id | AG4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 712 |
| Chain | Residue |
| B | PHE434 |
| B | HIS461 |
| B | LEU466 |
| B | ASP469 |
| B | HIS473 |
| B | HOH1093 |
| site_id | AG5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 713 |
| Chain | Residue |
| B | ALA271 |
| B | ARG274 |
| B | GLU275 |
| B | EDO703 |
| B | EDO704 |
| B | HOH933 |
| B | HOH1025 |
| B | HOH1397 |
| site_id | AG6 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 714 |
| Chain | Residue |
| B | LEU45 |
| B | LYS46 |
| B | HIS47 |
| B | ALA296 |
| B | ALA299 |
| B | LYS303 |
| B | HOH823 |
| B | HOH1049 |
| B | HOH1363 |
| site_id | AG7 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 715 |
| Chain | Residue |
| B | LEU435 |
| B | ASP462 |
| B | PRO475 |
| B | VAL479 |
| B | ARG492 |
| B | GLU612 |
| B | ALA613 |
| B | GLY614 |
| B | HOH1053 |
| site_id | AG8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 716 |
| Chain | Residue |
| B | LYS394 |
| B | ALA395 |
| B | GLU398 |
| B | HIS406 |
| B | HOH979 |
| site_id | AG9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 717 |
| Chain | Residue |
| B | ILE246 |
| B | PHE249 |
| B | GLY250 |
| B | ALA255 |
| B | GLN276 |
| B | HOH912 |
| B | HOH1306 |
| site_id | AH1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 718 |
| Chain | Residue |
| B | SER53 |
| B | MET329 |
| B | EDO711 |
| B | HOH805 |
| B | HOH1267 |
| site_id | AH2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 719 |
| Chain | Residue |
| A | EDO724 |
| A | HOH806 |
| A | HOH1099 |
| A | HOH1339 |
| B | ASP399 |
| site_id | AH3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 720 |
| Chain | Residue |
| B | PRO52 |
| B | VAL103 |
| B | VAL109 |
| B | HOH848 |
| B | HOH945 |
| B | HOH1004 |
| site_id | AH4 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 721 |
| Chain | Residue |
| A | ASP469 |
| B | SER24 |
| B | GLY25 |
| B | HIS26 |
| B | ARG91 |
| B | GLY262 |
| B | HOH909 |
| B | HOH984 |
| B | HOH1040 |
| site_id | AH5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 722 |
| Chain | Residue |
| A | THR198 |
| A | HOH1082 |
| B | GLY171 |
| B | HOH968 |
| B | HOH1164 |
| B | HOH1271 |
| site_id | AH6 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 723 |
| Chain | Residue |
| B | GLY176 |
| B | ALA231 |
| B | VAL234 |
| B | HOH998 |
| B | HOH1033 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17914867","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17914867","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-1999","submissionDatabase":"PDB data bank","title":"Crystal structure of Escherichia coli transketolase.","authors":["Isupov M.N.","Rupprecht M.P.","Wilson K.S.","Dauter Z.","Littlechild J.A."]}},{"source":"PDB","id":"1QGD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2R5N","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17914867","evidenceCode":"ECO:0000305"},{"source":"Reference","evidenceCode":"ECO:0000305","citation":{"citationType":"submission","publicationDate":"APR-1999","submissionDatabase":"PDB data bank","title":"Crystal structure of Escherichia coli transketolase.","authors":["Isupov M.N.","Rupprecht M.P.","Wilson K.S.","Dauter Z.","Littlechild J.A."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-1999","submissionDatabase":"PDB data bank","title":"Crystal structure of Escherichia coli transketolase.","authors":["Isupov M.N.","Rupprecht M.P.","Wilson K.S.","Dauter Z.","Littlechild J.A."]}},{"source":"PDB","id":"1QGD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17914867","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"APR-1999","submissionDatabase":"PDB data bank","title":"Crystal structure of Escherichia coli transketolase.","authors":["Isupov M.N.","Rupprecht M.P.","Wilson K.S.","Dauter Z.","Littlechild J.A."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalytic activity"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
