6TJ8
Escherichia coli transketolase in complex with cofactor analog 2'-methoxythiamine diphosphate
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 | 26 |
| Details | binding site for residue NDQ A 701 |
| Chain | Residue |
| A | ALA29 |
| A | ASN185 |
| A | ILE187 |
| A | ILE189 |
| A | ILE247 |
| A | HIS261 |
| A | CA702 |
| A | EDO714 |
| A | HOH807 |
| A | HOH815 |
| A | HOH877 |
| A | HIS66 |
| A | HOH948 |
| A | HOH1169 |
| B | ASP381 |
| B | GLU411 |
| B | PHE437 |
| B | TYR440 |
| B | HIS473 |
| A | GLY114 |
| A | PRO115 |
| A | LEU116 |
| A | GLY154 |
| A | ASP155 |
| A | GLY156 |
| A | GLU160 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 702 |
| Chain | Residue |
| A | ASP155 |
| A | ASN185 |
| A | ILE187 |
| A | NDQ701 |
| A | HOH948 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 703 |
| Chain | Residue |
| A | PHE375 |
| A | TRP390 |
| A | SER393 |
| A | ASN403 |
| A | TYR404 |
| A | TYR430 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 704 |
| Chain | Residue |
| A | SER559 |
| A | GLU560 |
| A | PHE645 |
| A | HOH840 |
| A | HOH1236 |
| A | HOH1273 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 705 |
| Chain | Residue |
| A | LEU45 |
| A | LYS46 |
| A | HIS47 |
| A | LYS303 |
| A | HOH1073 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 706 |
| Chain | Residue |
| A | ILE615 |
| A | ASP617 |
| A | THR633 |
| A | HOH1345 |
| A | HOH1375 |
| B | ARG483 |
| B | HOH839 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 707 |
| Chain | Residue |
| A | LEU435 |
| A | ASP462 |
| A | PRO475 |
| A | VAL479 |
| A | ARG492 |
| A | GLU612 |
| A | ALA613 |
| A | GLY614 |
| A | HOH1079 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | binding site for residue EDO A 708 |
| Chain | Residue |
| A | HIS47 |
| A | ARG57 |
| A | ASP58 |
| A | PHE60 |
| A | TYR80 |
| A | GLY108 |
| A | GLU110 |
| A | HOH825 |
| A | HOH839 |
| A | HOH1072 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 709 |
| Chain | Residue |
| A | THR326 |
| A | HOH963 |
| A | HOH1175 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 710 |
| Chain | Residue |
| A | HOH812 |
| A | HOH1322 |
| A | HOH1361 |
| B | ASP399 |
| B | HOH988 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 711 |
| Chain | Residue |
| A | ARG4 |
| A | ARG42 |
| A | GLN293 |
| A | HOH915 |
| A | HOH995 |
| B | GLY392 |
| B | LYS394 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 712 |
| Chain | Residue |
| A | TYR620 |
| A | GLY624 |
| A | LEU625 |
| A | ASN626 |
| A | GLY627 |
| A | HOH816 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 713 |
| Chain | Residue |
| A | HOH1038 |
| A | HOH1140 |
| A | LYS131 |
| A | THR172 |
| A | LYS174 |
| A | ASN397 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue EDO A 714 |
| Chain | Residue |
| A | HIS26 |
| A | ILE189 |
| A | HIS261 |
| A | NDQ701 |
| A | HOH807 |
| A | HOH1318 |
| B | PHE434 |
| B | ASP469 |
| B | HIS473 |
| B | HOH821 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 715 |
| Chain | Residue |
| A | GLN526 |
| A | GLU527 |
| A | LYS544 |
| A | VAL565 |
| A | HOH931 |
| A | HOH1305 |
| site_id | AD7 |
| Number of Residues | 9 |
| Details | binding site for residue EDO A 716 |
| Chain | Residue |
| A | TYR182 |
| A | ASP184 |
| A | PHE197 |
| A | THR198 |
| A | ASP199 |
| A | THR201 |
| A | HOH917 |
| A | HOH1054 |
| A | HOH1460 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 717 |
| Chain | Residue |
| A | PHE434 |
| A | HIS461 |
| A | LEU466 |
| A | ASP469 |
| A | HIS473 |
| A | ARG520 |
| B | EDO711 |
| B | HOH894 |
| site_id | AD9 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 718 |
| Chain | Residue |
| A | GLN136 |
| A | PHE137 |
| A | ARG139 |
| A | HOH833 |
| A | HOH855 |
| A | HOH955 |
| A | HOH1104 |
| site_id | AE1 |
| Number of Residues | 27 |
| Details | binding site for residue NDQ B 701 |
| Chain | Residue |
| A | ASP381 |
| A | GLU411 |
| A | PHE437 |
| A | TYR440 |
| A | HIS473 |
| A | HOH1245 |
| B | ALA29 |
| B | HIS66 |
| B | GLY114 |
| B | PRO115 |
| B | LEU116 |
| B | GLY154 |
| B | ASP155 |
| B | GLY156 |
| B | GLU160 |
| B | ASN185 |
| B | ILE187 |
| B | ILE189 |
| B | ILE247 |
| B | HIS261 |
| B | CA702 |
| B | EDO711 |
| B | HOH816 |
| B | HOH874 |
| B | HOH935 |
| B | HOH1125 |
| B | HOH1207 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 702 |
| Chain | Residue |
| B | ASP155 |
| B | ASN185 |
| B | ILE187 |
| B | NDQ701 |
| B | HOH935 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 703 |
| Chain | Residue |
| B | PHE375 |
| B | TRP390 |
| B | SER393 |
| B | ASN403 |
| B | TYR404 |
| B | TYR430 |
| B | HOH1163 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 704 |
| Chain | Residue |
| B | ALA271 |
| B | TYR505 |
| B | GLU508 |
| B | ARG509 |
| B | EDO714 |
| B | HOH891 |
| B | HOH970 |
| site_id | AE5 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 705 |
| Chain | Residue |
| B | ARG274 |
| B | GLU275 |
| B | TRP279 |
| B | ARG538 |
| B | GLN592 |
| B | EDO714 |
| B | HOH893 |
| B | HOH985 |
| B | HOH1072 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 706 |
| Chain | Residue |
| B | LEU272 |
| B | GLU275 |
| B | ARG509 |
| B | ASP511 |
| B | HOH1078 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 707 |
| Chain | Residue |
| B | LYS21 |
| B | LYS88 |
| B | GLN92 |
| B | HOH852 |
| B | HOH865 |
| B | HOH932 |
| site_id | AE8 |
| 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 | HOH1101 |
| site_id | AE9 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 709 |
| Chain | Residue |
| B | LEU435 |
| B | ASP462 |
| B | PRO475 |
| B | VAL479 |
| B | ARG492 |
| B | GLU612 |
| B | ALA613 |
| B | GLY614 |
| B | HOH1077 |
| site_id | AF1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 710 |
| Chain | Residue |
| B | SER559 |
| B | GLU560 |
| B | PHE645 |
| B | PHE650 |
| B | HOH845 |
| B | HOH1073 |
| site_id | AF2 |
| Number of Residues | 11 |
| Details | binding site for residue EDO B 711 |
| Chain | Residue |
| A | ASP469 |
| A | EDO717 |
| A | HOH821 |
| A | HOH1245 |
| B | HIS26 |
| B | ILE189 |
| B | HIS261 |
| B | NDQ701 |
| B | EDO718 |
| B | HOH823 |
| B | HOH1283 |
| site_id | AF3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 712 |
| Chain | Residue |
| B | THR326 |
| B | HOH983 |
| B | HOH1440 |
| site_id | AF4 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 713 |
| Chain | Residue |
| B | TYR182 |
| B | ASP184 |
| B | PHE197 |
| B | THR198 |
| B | ASP199 |
| B | THR201 |
| B | HOH801 |
| B | HOH951 |
| B | HOH1160 |
| site_id | AF5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 714 |
| Chain | Residue |
| B | ALA271 |
| B | GLU275 |
| B | EDO704 |
| B | EDO705 |
| B | HOH990 |
| B | HOH1114 |
| B | HOH1355 |
| site_id | AF6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 715 |
| Chain | Residue |
| B | LYS131 |
| B | THR172 |
| B | LYS174 |
| B | HOH987 |
| B | HOH1018 |
| B | HOH1062 |
| site_id | AF7 |
| Number of Residues | 11 |
| Details | binding site for residue EDO B 716 |
| Chain | Residue |
| B | LEU45 |
| B | HIS47 |
| B | ARG57 |
| B | ASP58 |
| B | PHE60 |
| B | TYR80 |
| B | GLY108 |
| B | GLU110 |
| B | HOH810 |
| B | HOH826 |
| B | HOH1028 |
| site_id | AF8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 717 |
| Chain | Residue |
| B | ILE246 |
| B | PHE249 |
| B | GLY250 |
| B | ALA255 |
| B | GLN276 |
| B | HOH940 |
| site_id | AF9 |
| Number of Residues | 10 |
| Details | binding site for residue EDO B 718 |
| Chain | Residue |
| A | ASP469 |
| B | SER24 |
| B | GLY25 |
| B | HIS26 |
| B | ARG91 |
| B | GLY262 |
| B | EDO711 |
| B | HOH823 |
| B | HOH894 |
| B | HOH1133 |
| site_id | AG1 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 719 |
| Chain | Residue |
| A | PHE635 |
| B | ALA449 |
| B | LEU450 |
| B | LYS452 |
| B | ASN487 |
| B | HOH848 |
| B | HOH1015 |
| B | HOH1094 |
| B | HOH1332 |
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 |
