1DSU

HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME

Summary for 1DSU

• Entry DOI: 10.2210/pdb1dsu/pdb
• Descriptor: FACTOR D (2 entities in total)
• Functional Keywords: complement activating enzyme, hydrolase, serine protease, hydrolase (serine protease)
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P00746
• Total number of polymer chains: 2
• Total formula weight: 48877.61

Authors

Narayana, S.V.L.,Volanakis, J.E.,Delucas, L.J. (deposition date: 1995-09-15, release date: 1996-08-17, Last modification date: 2024-10-23)

Primary citation

Narayana, S.V.,Carson, M.,el-Kabbani, O.,Kilpatrick, J.M.,Moore, D.,Chen, X.,Bugg, C.E.,Volanakis, J.E.,DeLucas, L.J.
Structure of human factor D. A complement system protein at 2.0 A resolution.
J.Mol.Biol., 235:695-708, 1994

PubMed Abstract: 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.

PubMed: 8289289
DOI: 10.1006/jmbi.1994.1021

Experimental method

X-RAY DIFFRACTION (2 Å)