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Table of contents
  1. 1. Welcome to TOPSAN
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Welcome to TOPSAN

The TOPSAN project was developed to collect, share, and distribute information about protein three-dimensional structures. TOPSAN serves as a portal for the scientific community to learn about protein structures solved by SG centers, and also to contribute their expertise in annotating protein function. 

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  FEATURED ANNOTATION
2q9k:

The Exig_1997 gene from Exiguobacterium sibiricum 255-15 gives several strong, but possibly misleading hints to encode for a pyridoxamine 5'-phosphate oxidase (PF01243, cl00381), an enzyme which catalyzes the reaction of pyridoxamine-5-P (PMP) and pyridoxine-5-P (PNP) to pyridoxal-5-P (PLP). The structure adopts a beta roll (2q9k-CATH). There is high structural similarity to several oxidoreductases like 1r1z [Ref] and PSI target 2ou5. Significant sequence homology to 2e83 (chain A), 3f7e (chain A) is detected by HHpred. ...


TOPSAN - The Network News
New TOPSAN Paper and Download Details
A paper on TOPSAN, entitled: “TOPSAN: a dynamic web database for structural genomics” will be featured in the Nucleic Acids Research upcoming database issue. One of the main points of this paper is the many efforts to make TOPSAN data more accessible. These efforts include providing TOPSAN articles for bulk download in machine readable formats. [...]
TOPSAN and the Semantic Web (Part II)
This is the second in a series of blogs in which we will try to introduce you to the concepts behind the TOPSAN Protein Syntax and the TOPSAN semantic notation system. Our first entry introduced how to imbed semantic web notations into TOPSAN (Part I). In this article we will describe how to use obtain [...]
 

 

RECENT ARTICLES
Nucleic Acids Research
TOPSAN: a dynamic web database for structural genomics (2010)Read article


BMC Bioinformatics
TOPSAN: a collaborative annotation environment for structural genomics. (2010) Read article


Acta Crystal. F
TOPSAN: use of a collaborative environment for annotating, analyzing and disseminating data on JCSG and PSI structures. Acta Cryst. (2010) 66:1143-1147, Read article

 

Reviews

References

 

  1. van den Heuvel RH, Westphal AH, Heck AJ, Walsh MA, Rovida S, van Berkel WJ, and Mattevi A Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action. J Biol Chem. 2004 Mar 26; 279(13):12860-7 PubMed HubMed doi:10.1074/jbc.M313765200 pmid:14703520.

     


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