1EO5
Bacillus circulans strain 251 cyclodextrin glycosyltransferase in complex with maltoheptaose
Summary for 1EO5
Entry DOI | 10.2210/pdb1eo5/pdb |
Related | 1CDG 1cxf 1CXI 1CXK 1CXL 1d3C 1EO7 |
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 Cited by PubMed: 10869182DOI: 10.1021/bi000340x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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