1dsu: Difference between revisions

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[[Image:1dsu.gif|left|200px]]
{{Seed}}
[[Image:1dsu.png|left|200px]]


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{{STRUCTURE_1dsu|  PDB=1dsu  |  SCENE=  }}  
{{STRUCTURE_1dsu|  PDB=1dsu  |  SCENE=  }}  


'''HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME'''
===HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME===




==Overview==
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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.
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{{ABSTRACT_PUBMED_8289289}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Serine protease]]
[[Category: Serine protease]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:13:59 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:33:53 2008''

Revision as of 20:33, 30 June 2008

File:1dsu.png

Template:STRUCTURE 1dsu

HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME

Template:ABSTRACT PUBMED 8289289

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

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