Arylformamidase Function Slide 5: Difference between revisions

Revision as of 12:30, 8 June 2008

- Catalytic triad identified in paper - Ser154, Asp251, and His281.

- To assess functional similarity, conservation of the catalytic triad was analysed.

Conservation of the catalytic triad between 2cb7 and 2pbl.

- Catalytic triad conserved.

- Note: difference in clustalW alignment from DALI sequence alignment. Unstable region of alignment?

@@ Line 1: / Line 1: @@
-== Thermostable? ==
+== Evidence from Similar Structures ==
-'''Structural similarity'''
+- Catalytic triad identified in paper - Ser154, Asp251, and His281.
-  No:  Chain   Z    rmsd lali nres  %id  Description
+- To assess functional similarity, conservation of the catalytic triad was analysed.
-:  2pbl-A 52.4  0.0  262   262  100   MOLECULE: PUTATIVE ESTERASE/LIPASE/THIOESTERASE;
-:  2c7b-A 23.4  3.0  231   294   16   MOLECULE: CARBOXYLESTERASE;
-:  1jji-A 23.0  3.1  233   311   15   MOLECULE: CARBOXYLESTERASE;
-:  1evq-A 21.4  2.9  225   308   18   MOLECULE: SERINE HYDROLASE;
-'''Sequence similarity'''
+[[Image:2c7b_alignment.png|centre|framed|'''Conservation of the catalytic triad between 2cb7 and 2pbl.''']]
-[[Image:HSL_alignment.png|centre|framed|'''Alignment with thermophillic HSL family members identified by Byun 2007.''']]
+- Catalytic triad conserved.
-'''Ecology''' - an aquatic organism widely present throughout world's oceans.
+- Note: difference in clustalW alignment from DALI sequence alignment. Unstable region of alignment?
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