1EO5

Bacillus circulans strain 251 cyclodextrin glycosyltransferase in complex with maltoheptaose

Summary for 1EO5

• Entry DOI: 10.2210/pdb1eo5/pdb
• Related: 1CDG 1CXI 1CXK 1CXL 1EO7 1cxf 1d3C
• Related PRD ID: PRD_900009 PRD_900010
• Descriptor: PROTEIN (CYCLODEXTRIN GLYCOSYLTRANSFERASE), alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: alpha-amylase, maltoheptaose, oligosaccharide, family 13 glycosyl hydrolase, transglycosylation, induced fit, catalysis, transferase
• Biological source: Bacillus circulans
• Total number of polymer chains: 1
• Total formula weight: 77686.38

Authors

Uitdehaag, J.C.M.,Dijkstra, B.W. (deposition date: 2000-03-22, release date: 2000-11-22, Last modification date: 2023-08-09)

• Primary citation: Uitdehaag, J.C.,van Alebeek, G.J.,van Der Veen, B.A.,Dijkhuizen, L.,Dijkstra, B.W.; Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.; Biochemistry, 39:7772-7780, 2000; PubMed: 10869182; DOI: 10.1021/bi000340x

Experimental method

X-RAY DIFFRACTION (2 Å)