1M3U
Crystal Structure of Ketopantoate Hydroxymethyltransferase complexed the Product Ketopantoate
Summary for 1M3U
Entry DOI | 10.2210/pdb1m3u/pdb |
Descriptor | 3-methyl-2-oxobutanoate hydroxymethyltransferase, MAGNESIUM ION, KETOPANTOATE, ... (4 entities in total) |
Functional Keywords | beta-alpha-barrel, tim-barrel, ketopantoate, selenomethionine mad, decamer, transferase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm : P31057 |
Total number of polymer chains | 10 |
Total formula weight | 284348.23 |
Authors | von Delft, F.,Inoue, T.,Saldanha, S.A.,Ottenhof, H.H.,Dhanaraj, V.,Witty, M.,Abell, C.,Smith, A.G.,Blundell, T.L. (deposition date: 2002-06-30, release date: 2003-07-22, Last modification date: 2024-04-03) |
Primary citation | von Delft, F.,Inoue, T.,Saldanha, S.A.,Ottenhof, H.H.,Schmitzberger, F.,Birch, L.M.,Dhanaraj, V.,Witty, M.,Smith, A.G.,Blundell, T.L.,Abell, C. Structure of E. coli Ketopantoate Hydroxymethyl Transferase Complexed with Ketopantoate and Mg(2+), Solved by Locating 160 Selenomethionine Sites. Structure, 11:985-996, 2003 Cited by PubMed: 12906829DOI: 10.1016/S0969-2126(03)00158-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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