Sandbox Reserved 1654: Difference between revisions

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***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***A <scene name='86/868187/Rd_turn/1'>Rubredoxin turn</scene> (Rd turn, residues 515-520), which is stabilized by hydrogen bonds between amide and sulfure.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***β-hairpin with <scene name='86/868187/B1/1'>β1</scene> (residues 525-527) and <scene name='86/868187/B2/1'>β2</scene> (residues 533-535) between which there is an helical turn stabilized by hydrogen bonds.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins.
***An <scene name='86/868187/A/1'>α1 helix</scene> (residues 538-545) which forms the second bridge between the two zinc-binding sites. The surface-exposed face of the helix has a potential for specific intermolecular interactions with nucleic acids or proteins. Therefore, it is this area that would be a platform to bind different proteins (ePAB, PARN, ...) by making hydrogen bonds. 
***A 3<sub>10</sub> <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***A 3<sub>10</sub> <scene name='86/868187/310/1'> helical turn</scene> (residues 550-552).
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.
***2 zinc binding sites, the first one is composed of <scene name='86/868187/Z1/3'>Cys515, Cys518, Cys537, Cys540</scene> and the second is composed of <scene name='86/868187/Z2/2'>Cys527, Cys532, His545 and His553</scene>.