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1kct

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[[Image:1kct.jpg|left|200px]]
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{{Structure
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|PDB= 1kct |SIZE=350|CAPTION= <scene name='initialview01'>1kct</scene>, resolution 3.46&Aring;
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|SITE= <scene name='pdbsite=P1:Reactive+Site+In+Inhibitory+Loop'>P1</scene>
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|GENE= A1AT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1kct| PDB=1kct | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kct OCA], [http://www.ebi.ac.uk/pdbsum/1kct PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kct RCSB]</span>
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'''ALPHA1-ANTITRYPSIN'''
'''ALPHA1-ANTITRYPSIN'''
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[[Category: Serine protease inhibitor]]
[[Category: Serine protease inhibitor]]
[[Category: Serpin]]
[[Category: Serpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:35:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Apr 5 19:09:51 2008''
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Revision as of 19:35, 2 May 2008

Image:1kct.jpg

Template:STRUCTURE 1kct

ALPHA1-ANTITRYPSIN


Overview

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].

About this Structure

1KCT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of an uncleaved alpha 1-antitrypsin reveals the conformation of its inhibitory reactive loop., Song HK, Lee KN, Kwon KS, Yu MH, Suh SW, FEBS Lett. 1995 Dec 18;377(2):150-4. PMID:8543039 Page seeded by OCA on Fri May 2 22:35:02 2008

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