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1W3D

NMR structure of the peripheral-subunit binding domain of Bacillus stearothermophilus E2p

Summary for 1W3D
Entry DOI10.2210/pdb1w3d/pdb
Related1B5S 1EBD 1LAB 1LAC 2PDD 2PDE
DescriptorDIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE (1 entity in total)
Functional Keywordstransferase, peripheral-subunit binding domain, dihydrolipoamide acetyltransferase, dihydrolipoamide dehydrogenase, protein- protein interaction, protein structure, multienzyme complex, bacillus sterothermophilus, glycolysis, acyltransferase, lipoyl
Biological sourceGEOBACILLUS STEAROTHERMOPHILUS
Total number of polymer chains1
Total formula weight5806.62
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 citationAllen, 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: 15634348
DOI: 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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