1W3D
NMR structure of the peripheral-subunit binding domain of Bacillus stearothermophilus E2p
Summary for 1W3D
Entry DOI | 10.2210/pdb1w3d/pdb |
Related | 1B5S 1EBD 1LAB 1LAC 2PDD 2PDE |
Descriptor | DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE (1 entity in total) |
Functional Keywords | transferase, peripheral-subunit binding domain, dihydrolipoamide acetyltransferase, dihydrolipoamide dehydrogenase, protein- protein interaction, protein structure, multienzyme complex, bacillus sterothermophilus, glycolysis, acyltransferase, lipoyl |
Biological source | GEOBACILLUS STEAROTHERMOPHILUS |
Total number of polymer chains | 1 |
Total formula weight | 5806.62 |
Authors | Allen, M.D.,Broadhurst, R.W.,Solomon, R.G.,Perham, R.N. (deposition date: 2004-07-14, release date: 2004-07-20, Last modification date: 2018-01-24) |
Primary citation | Allen, M.D.,Broadhurst, R.W.,Solomon, R.G.,Perham, R.N. Interaction of the E2 and E3 Components of the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus Stearothermophilus. Use of a Truncated Protein Domain in NMR Spectroscopy FEBS J., 272:259-, 2005 Cited by PubMed: 15634348DOI: 10.1111/J.1432-1033.2004.04405.X PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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