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: 19232354 DOI: 10.1016/j.jmb.2009.01.069 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation