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1f13
From Proteopedia
=ARIJIT BISWAS page for Factor XIII protein=
| 1f13, resolution 2.10Å () | |||||||||
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| Sites: | and | ||||||||
| Activity: | Protein-glutamine gamma-glutamyltransferase, with EC number 2.3.2.13 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
RECOMBINANT HUMAN CELLULAR COAGULATION FACTOR XIII
The A subunit is composed of an activation peptide and 4 domains: the β-sandwich , the central core domain, the barrel 1 domain, and the .
The structure of recombinant human cellular factor XIII zymogen was solved in its monoclinic crystal form and refined to an R-factor of 18.3% (Rfree = 23.6%) for all data between 40.0 and 2.1 A resolution. Two non-proline cis peptide bonds were detected. One is between Arg310 and Tyr311 close to the active site cysteine residue (Cys314) and the other is between Gln425 and Phe426 at the dimerization interface. The structure and the role of these cis peptides are discussed in the light of their possible importance for factor XIII function.
Two non-proline cis peptide bonds may be important for factor XIII function., Weiss MS, Metzner HJ, Hilgenfeld R, FEBS Lett. 1998 Feb 27;423(3):291-6. PMID:9515726
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1F13 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Weblinks
Reference
- Weiss MS, Metzner HJ, Hilgenfeld R. Two non-proline cis peptide bonds may be important for factor XIII function. FEBS Lett. 1998 Feb 27;423(3):291-6. PMID:9515726
Page seeded by OCA on Tue Feb 17 11:54:21 2009
