2GJP
Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose
Summary for 2GJP
Entry DOI | 10.2210/pdb2gjp/pdb |
Related | 1W9X 2GJR |
Related PRD ID | PRD_900001 |
Descriptor | alpha-amylase, 4,6-dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5-enopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, 4,6-dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5-enopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (8 entities in total) |
Functional Keywords | alpha-amylase, maltose binding site, bacillus halmapalus, hydrolase |
Biological source | Bacillus halmapalus |
Total number of polymer chains | 1 |
Total formula weight | 58028.28 |
Authors | Lyhne-Iversen, L.,Hobley, T.J.,Kaasgaard, S.G.,Harris, P. (deposition date: 2006-03-31, release date: 2006-09-05, Last modification date: 2023-08-30) |
Primary citation | Lyhne-Iversen, L.,Hobley, T.J.,Kaasgaard, S.G.,Harris, P. Structure of Bacillus halmapalus alpha-amylase crystallized with and without the substrate analogue acarbose and maltose. Acta Crystallogr.,Sect.F, 62:849-854, 2006 Cited by PubMed: 16946462DOI: 10.1107/S174430910603096X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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