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; PubMed: 16946462; DOI: 10.1107/S174430910603096X

Experimental method

X-RAY DIFFRACTION (1.9 Å)