3G7W
Islet Amyloid Polypeptide (IAPP or Amylin) Residues 1 to 22 fused to Maltose Binding Protein
Summary for 3G7W
Entry DOI | 10.2210/pdb3g7w/pdb |
Related | 3G7V |
Related PRD ID | PRD_900009 |
Descriptor | Maltose-binding periplasmic protein, Islet amyloid polypeptide fusion protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (5 entities in total) |
Functional Keywords | native fold for amyloidogenic protein, sugar transport, transport, amidation, amyloid, cleavage on pair of basic residues, hormone, secreted, sugar binding protein |
Biological source | Escherichia coli More |
Total number of polymer chains | 1 |
Total formula weight | 45539.45 |
Authors | Wiltzius, J.J.W.,Sawaya, M.R.,Eisenberg, D. (deposition date: 2009-02-11, release date: 2009-06-23, Last modification date: 2023-09-06) |
Primary citation | Wiltzius, J.J.,Sievers, S.A.,Sawaya, M.R.,Eisenberg, D. Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process Protein Sci., 18:1521-1530, 2009 Cited by PubMed: 19475663DOI: 10.1002/pro.145 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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