1URD
X-ray structures of the maltose-maltodextrin binding protein of the thermoacidophilic bacterium Alicyclobacillus acidocaldarius provide insight into acid stability of proteins
Summary for 1URD
Entry DOI | 10.2210/pdb1urd/pdb |
Related | 1URG 1URS |
Related PRD ID | PRD_900009 |
Descriptor | MALTOSE-BINDING PROTEIN, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total) |
Functional Keywords | maltose-binding protein, maltodextrin-binding protein, acidophile, thermoacidophile, hyperthermophile, thermophile |
Biological source | ALICYCLOBACILLUS ACIDOCALDARIUS |
Total number of polymer chains | 2 |
Total formula weight | 81784.30 |
Authors | Schafer, K.,Magnusson, U.,Scheffel, F.,Schiefner, A.,Sandgren, M.O.J.,Diederichs, K.,Welte, W.,Hulsmann, A.,Schneider, E.,Mowbray, S.L. (deposition date: 2003-10-29, release date: 2003-12-11, Last modification date: 2024-05-08) |
Primary citation | Schafer, K.,Magnusson, U.,Scheffel, F.,Schiefner, A.,Sandgren, M.O.J.,Diederichs, K.,Welte, W.,Hulsmann, A.,Schneider, E.,Mowbray, S.L. X-Ray Structures of the Maltose-Maltodextrin-Binding Protein of the Thermoacidophilic Bacterium Alicyclobacillus Acidocaldarius Provide Insight Into Acid Stability of Proteins. J.Mol.Biol., 335:261-, 2004 Cited by PubMed: 14659755DOI: 10.1016/J.JMB.2003.10.042 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.53 Å) |
Structure validation
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