ADP-ribose pyrophosphatase
From Proteopedia
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| - | + | <StructureSection load='1khz' size='450' side='right' scene='' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'> | |
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== Function == | == Function == | ||
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ADPRP contains two domains: the N-terminal domain responsible for dimer stabilization and the C-terminal which contains the active site. The C-terminal domain contains the Nudix (Nucleoside Diphosphate linked to X) sequence which is typical to pyrophosphatases and binds the metal ion. Residues from both monomers of ADPRP participate in the active site. | ADPRP contains two domains: the N-terminal domain responsible for dimer stabilization and the C-terminal which contains the active site. The C-terminal domain contains the Nudix (Nucleoside Diphosphate linked to X) sequence which is typical to pyrophosphatases and binds the metal ion. Residues from both monomers of ADPRP participate in the active site. | ||
| - | + | </StructureSection> | |
==3D structures of ADP-ribose pyrophosphatase== | ==3D structures of ADP-ribose pyrophosphatase== | ||
Revision as of 09:35, 3 November 2015
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3D structures of ADP-ribose pyrophosphatase
Updated on 03-November-2015
