User:Tilman Schirmer/Sandbox 202
From Proteopedia
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<scene name='User:Tilman_Schirmer/Sandbox_202/Yuki_dimer/3'>YukI</scene> is a dimer with each protomer composed of an <scene name='User:Tilman_Schirmer/Sandbox_202/Eal_domain/1'>EAL domain</scene>, a long <scene name='User:Tilman_Schirmer/Sandbox_202/Connection/1'>helical linker</scene>, and a <scene name='User:Tilman_Schirmer/Sandbox_202/Pas_like_domain/1'>PAS-like domain</scene>. <br> | <scene name='User:Tilman_Schirmer/Sandbox_202/Yuki_dimer/3'>YukI</scene> is a dimer with each protomer composed of an <scene name='User:Tilman_Schirmer/Sandbox_202/Eal_domain/1'>EAL domain</scene>, a long <scene name='User:Tilman_Schirmer/Sandbox_202/Connection/1'>helical linker</scene>, and a <scene name='User:Tilman_Schirmer/Sandbox_202/Pas_like_domain/1'>PAS-like domain</scene>. <br> | ||
| - | The <scene name='User:Tilman_Schirmer/Sandbox_202/ | + | The <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close/4'>active site </scene> is situated at the C-terminal end of the central β-barrel of the EAL domain (with TIM fold). The residues of the <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close_labels/1'>active site</scene> are well conserved, including E33 and L35 of the EAL signature motif. <br> |
| - | <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close/4'>Active site (Q19, E33, L35, R37, N88, E122, P152, K173, Q209)</scene> | ||
<scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close_labels/1'>Active site with labels</scene> | <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close_labels/1'>Active site with labels</scene> | ||
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<br><br><br><br><br><br><br><br><br> | <br><br><br><br><br><br><br><br><br> | ||
| + | <scene name='User:Tilman_Schirmer/Sandbox_202/Active_site_close/4'>Active site (Q19, E33, L35, R37, N88, E122, P152, K173, Q209)</scene> | ||
== BlrP1 == | == BlrP1 == | ||
Revision as of 20:51, 30 June 2009
C-di-GMP specific phosphodiesterases
YukI
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is a dimer with each protomer composed of an , a long , and a .
The is situated at the C-terminal end of the central β-barrel of the EAL domain (with TIM fold). The residues of the are well conserved, including E33 and L35 of the EAL signature motif.
BlrP1
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