1W85
The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain of E2
Summary for 1W85
Entry DOI | 10.2210/pdb1w85/pdb |
Related | 1B5S 1EBD 1LAB 1LAC 1W3D 1W4E 1W4F 1W4G 1W4H 1W88 2PDD 2PDE |
Descriptor | PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT, PYRUVATE DEHYDROGENASE E1 COMPONENT, BETA SUBUNIT, DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE, ... (8 entities in total) |
Functional Keywords | pyruvate, dehydrogenase, dihydrolipoyl, acetyl transferase, multienzyme complex, oxidoreductase, transferase |
Biological source | GEOBACILLUS STEAROTHERMOPHILUS More |
Total number of polymer chains | 10 |
Total formula weight | 319851.73 |
Authors | Frank, R.A.W.,Pratap, J.V.,Pei, X.Y.,Perham, R.N.,Luisi, B.F. (deposition date: 2004-09-16, release date: 2004-11-02, Last modification date: 2023-12-13) |
Primary citation | Frank, R.A.,Titman, C.M.,Pratap, J.V.,Luisi, B.F.,Perham, R.N. A molecular switch and proton wire synchronize the active sites in thiamine enzymes. Science, 306:872-876, 2004 Cited by PubMed: 15514159DOI: 10.1126/science.1101030 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report