3DRM
2.2 Angstrom Crystal Structure of Thr114Phe Alpha1-Antitrypsin
Summary for 3DRM
Entry DOI | 10.2210/pdb3drm/pdb |
Related | 3DRU |
Descriptor | Alpha-1-antitrypsin (2 entities in total) |
Functional Keywords | serpin, serine proteinase inhibitor, alpha1-antitrypsin, polymerisation, rational drug design, conformational disease, emphysema, cirrhosis, acute phase, alternative splicing, blood coagulation, disease mutation, glycoprotein, hydrolase, polymorphism, protease, protease inhibitor, secreted, serine protease inhibitor, hydrolase inhibitor |
Biological source | Homo sapiens (human) |
Cellular location | Secreted. Short peptide from AAT: Secreted, extracellular space, extracellular matrix: P01009 |
Total number of polymer chains | 1 |
Total formula weight | 45657.81 |
Authors | Gooptu, B.,Nobeli, I.,Purkiss, A.,Phillips, R.L.,Mallya, M.,Lomas, D.A.,Barrett, T.E. (deposition date: 2008-07-11, release date: 2009-03-31, Last modification date: 2023-08-30) |
Primary citation | Gooptu, B.,Miranda, E.,Nobeli, I.,Mallya, M.,Purkiss, A.,Brown, S.C.,Summers, C.,Phillips, R.L.,Lomas, D.A.,Barrett, T.E. Crystallographic and cellular characterisation of two mechanisms stabilising the native fold of alpha1-antitrypsin: implications for disease and drug design. J.Mol.Biol., 387:857-868, 2009 Cited by PubMed: 19232354DOI: 10.1016/j.jmb.2009.01.069 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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