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1kct
From Proteopedia
(New page: 200px<br /> <applet load="1kct" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kct, resolution 3.46Å" /> '''ALPHA1-ANTITRYPSIN'...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1KCT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KCT OCA]]. | + | 1KCT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Structure known Active Site: P1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KCT OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: serpin]] | [[Category: serpin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:45:16 2007'' |
Revision as of 11:40, 30 October 2007
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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]. Structure known Active Site: P1. 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
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