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: 2020-07-29)
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: 14659755 DOI: 10.1016/J.JMB.2003.10.042 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.53 Å)

Structure validation