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1dsu

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[[Image:1dsu.gif|left|200px]]
[[Image:1dsu.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1dsu", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Complement_factor_D Complement factor D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.46 3.4.21.46] </span>
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{{STRUCTURE_1dsu| PDB=1dsu | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dsu OCA], [http://www.ebi.ac.uk/pdbsum/1dsu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dsu RCSB]</span>
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'''HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME'''
'''HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME'''
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[[Category: Narayana, S V.L.]]
[[Category: Narayana, S V.L.]]
[[Category: Volanakis, J E.]]
[[Category: Volanakis, J E.]]
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[[Category: complement activating enzyme]]
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[[Category: Complement activating enzyme]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: serine protease]]
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[[Category: Serine protease]]
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Revision as of 11:13, 2 May 2008

Template:STRUCTURE 1dsu

HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME


Overview

Factor D, an essential enzyme for the activation of the alternative pathway of the complement system, belongs to the serine protease superfamily. The crystal structure of the enzyme was solved by a combination of multiple isomorphous replacement and molecular replacement methods. The present model was refined to an R-factor of 18.8% using 23,681 observed reflections between 7.5 and 2.0 A resolution, with a root-mean-square deviation from standard bond lengths of 0.016 A. The two non-crystallographically related molecules in the triclinic unit cell have distinctive active site conformations. The protein has the general structural fold of a serine protease, but there are several unique amino acid substitutions resulting in significant alterations in the critical loops responsible for catalysis and substrate specificity in serine proteases. Factor D is the first complement serine protease whose three-dimensional structure has been determined.

About this Structure

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

Reference

Structure of human factor D. A complement system protein at 2.0 A resolution., Narayana SV, Carson M, el-Kabbani O, Kilpatrick JM, Moore D, Chen X, Bugg CE, Volanakis JE, DeLucas LJ, J Mol Biol. 1994 Jan 14;235(2):695-708. PMID:8289289 Page seeded by OCA on Fri May 2 14:13:59 2008

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