1KCT
ALPHA1-ANTITRYPSIN
Summary for 1KCT
Entry DOI | 10.2210/pdb1kct/pdb |
Descriptor | ALPHA1-ANTITRYPSIN (1 entity in total) |
Functional Keywords | serpin, serine protease inhibitor, glycoprotein |
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 | 44304.28 |
Authors | Song, H.K.,Suh, S.W. (deposition date: 1996-08-06, release date: 1997-01-11, Last modification date: 2024-02-07) |
Primary citation | Song, H.K.,Lee, K.N.,Kwon, K.S.,Yu, M.H.,Suh, S.W. Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop. FEBS Lett., 377:150-154, 1995 Cited by PubMed Abstract: The crystal structure of a recombinant human alpha 1-antitrypsin, in the uncleaved and uncomplexed state, has been determined by X-ray crystallographic methods and refined to an R-factor of 18.4% for 8.0-3.46 A data with good stereochemistry. This structure provides the first view at the inhibitory loop and the central beta-sheet A of the uncleaved alpha 1-antitrypsin. The reactive loop takes a distorted helical conformation and no pre-insertion of two residues in the reactive loop into the beta-sheet A is observed. The present structure is largely in agreement with the model predicted by Engh, Wright, and Huber [Prot. Eng. 3 (1990) 469-477]. PubMed: 8543039DOI: 10.1016/0014-5793(95)01331-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.46 Å) |
Structure validation
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