Arylformamidase Function: Difference between revisions

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[[Image:Arylformamidase function.jpg]]
[[Image:Arylformamidase function.jpg]]


From the DALI output, 2cb7 was found to be the most similar structure to 2pbl having a Z-score of 23.4, 16% sequence identity and a root mean square deviation of 3.0. Conservation of the catalytic triad of 2cb7 as identified by ... was analysed for 2pbl (see figure 1).  
From the DALI output, 2c7b was found to be the most similar structure to 2pbl having a Z-score of 23.4, 16% sequence identity and a root mean square deviation of 3.0. Conservation of the catalytic triad of 2cb7 as identified by ... was analysed for 2pbl (see figure 1).  


  [[Image:2cb7alignment.jpg]]
  [[Image:2cb7alignment.jpg]]

Revision as of 10:01, 27 May 2008

Arylformamidase function.jpg

From the DALI output, 2c7b was found to be the most similar structure to 2pbl having a Z-score of 23.4, 16% sequence identity and a root mean square deviation of 3.0. Conservation of the catalytic triad of 2cb7 as identified by ... was analysed for 2pbl (see figure 1).

2cb7alignment.jpg
Figure 1: Conservation of the ... catalytic triad between 2cb7 and 2pbl.

A review of the DALI output revealed many structures similar to 2pbl with little sequence identity. The most similar of these, 2cb7, is a thermophilic and thermostable carboxylesterase. The catalytic triad responsible for its activity has been identified, and in determining whether 2pbl shared similar functionality, conservation of the catalytic triad between the two proteins was assessed (see figure 1).


Evidence from Similar Sequences

Arylformamidase alignment.jpg

Genomic Context

Cellular Context (location)

Species Similarities


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