2R8O
Transketolase from E. coli in complex with substrate D-xylulose-5-phosphate
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 | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 670 |
| Chain | Residue |
| A | ASP155 |
| A | ASN185 |
| A | ILE187 |
| A | T5X671 |
| A | HOH680 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 670 |
| Chain | Residue |
| B | HOH730 |
| B | ASP155 |
| B | ASN185 |
| B | ILE187 |
| B | T5X671 |
| site_id | AC3 |
| Number of Residues | 36 |
| Details | BINDING SITE FOR RESIDUE T5X A 671 |
| Chain | Residue |
| A | HIS26 |
| A | ALA29 |
| A | HIS66 |
| A | HIS100 |
| A | GLY114 |
| A | LEU116 |
| A | ASP155 |
| A | GLY156 |
| A | GLU160 |
| A | ASN185 |
| A | ILE187 |
| A | ILE189 |
| A | ILE247 |
| A | HIS261 |
| A | CA670 |
| A | HOH677 |
| A | HOH680 |
| A | HOH681 |
| A | HOH682 |
| A | HOH687 |
| A | HOH691 |
| A | HOH697 |
| A | HOH703 |
| A | HOH747 |
| A | HOH793 |
| B | ASP381 |
| B | SER385 |
| B | GLU411 |
| B | PHE434 |
| B | PHE437 |
| B | TYR440 |
| B | HIS461 |
| B | ASP469 |
| B | HIS473 |
| B | ARG520 |
| B | HOH1232 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE T5X B 671 |
| Chain | Residue |
| A | ASP381 |
| A | SER385 |
| A | GLU411 |
| A | PHE434 |
| A | PHE437 |
| A | TYR440 |
| A | HIS461 |
| A | ASP469 |
| A | HIS473 |
| A | ARG520 |
| A | HOH700 |
| A | HOH943 |
| B | HIS26 |
| B | ALA29 |
| B | HIS66 |
| B | HIS100 |
| B | GLY114 |
| B | LEU116 |
| B | ASP155 |
| B | GLY156 |
| B | GLU160 |
| B | ASN185 |
| B | ILE187 |
| B | ILE189 |
| B | ILE247 |
| B | HIS261 |
| B | CA670 |
| B | HOH682 |
| B | HOH690 |
| B | HOH693 |
| B | HOH695 |
| B | HOH699 |
| B | HOH736 |
| B | HOH763 |
| B | HOH1252 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 672 |
| Chain | Residue |
| B | GLU6 |
| B | GLY278 |
| B | TRP279 |
| B | LYS280 |
| B | TYR281 |
| B | HOH913 |
| B | HOH1215 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 673 |
| Chain | Residue |
| B | ALA271 |
| B | TYR505 |
| B | GLU508 |
| B | ARG509 |
| B | HOH783 |
| B | HOH816 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 674 |
| Chain | Residue |
| B | HOH1124 |
| B | HOH1224 |
| B | ARG274 |
| B | GLU275 |
| B | TRP279 |
| B | GLN592 |
| B | HOH822 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 675 |
| Chain | Residue |
| B | LEU272 |
| B | GLU275 |
| B | ARG509 |
| B | ASP511 |
| B | HOH1103 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 676 |
| Chain | Residue |
| B | PHE375 |
| B | TRP390 |
| B | SER393 |
| B | ASN403 |
| B | TYR404 |
| B | TYR430 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 677 |
| Chain | Residue |
| B | PRO52 |
| B | GLY108 |
| B | VAL109 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 672 |
| Chain | Residue |
| A | ILE615 |
| A | ASP617 |
| A | THR633 |
| A | HOH898 |
| B | ARG483 |
| B | HOH906 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 678 |
| Chain | Residue |
| B | SER559 |
| B | GLU560 |
| B | PHE645 |
| B | PHE650 |
| B | HOH917 |
| B | HOH1088 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 679 |
| Chain | Residue |
| B | LYS131 |
| B | THR172 |
| B | LYS174 |
| B | ASN397 |
| B | HOH842 |
| B | HOH1094 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 680 |
| Chain | Residue |
| B | LEU435 |
| B | ASP462 |
| B | PRO475 |
| B | VAL479 |
| B | ARG492 |
| B | ALA613 |
| B | GLY614 |
| B | HOH752 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 681 |
| Chain | Residue |
| B | PHE325 |
| B | THR326 |
| B | HOH881 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | SER251 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | HIS261 | |
| B | HIS26 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | SER251 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | GLU411 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | GLU411 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | PRO252 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | PRO252 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | HIS258 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| B | HIS258 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dtw |
| Chain | Residue | Details |
| A | HIS261 | |
| A | HIS26 |
