2AZD
X-Ray studies on Maltodextrin Phosphorylase (MalP) Complexes: recognition of substrates and CATALYTIC mechanism of phosphorylase family
Summary for 2AZD
Entry DOI | 10.2210/pdb2azd/pdb |
Related | 1l5v 1l5w 1l6i 1qm5 |
Descriptor | Maltodextrin phosphorylase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, VANADATE ION, ... (6 entities in total) |
Functional Keywords | maltopentaose, carbohydrate recognition, phosphorylase mechanism, ternary complexes with natural and inhibitory substrates, transferase |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 183395.73 |
Authors | Geremia, S.,Campagnolo, M. (deposition date: 2005-09-10, release date: 2005-09-20, Last modification date: 2021-11-10) |
Primary citation | Campagnolo, M.,Campa, C.,Zorzi, R.D.,Wuerges, J.,Geremia, S. X-ray studies on ternary complexes of maltodextrin phosphorylase. Arch.Biochem.Biophys., 471:11-19, 2008 Cited by PubMed: 18164678DOI: 10.1016/j.abb.2007.11.023 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.16 Å) |
Structure validation
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