Aspartate-semialdehyde dehydrogenase

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== Structural highlights ==
== Structural highlights ==
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ASADH contains 2 domains. The N terminal domain contains the <scene name='45/452498/Cv/3'>active site</scene> and the <scene name='45/452498/Cv/4'>NADP-binding site</scene>. The active site contains a <scene name='45/452498/Cv/5'>cysteine residue</scene> (C134, in olive) which binds to inhibitors. The C terminal contains the homodimer intersubunit contacts.
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ASADH contains 2 domains. The N terminal domain contains the <scene name='45/452498/Cv/3'>active site</scene> and the <scene name='45/452498/Cv/4'>NADP-binding site</scene>. The active site contains a <scene name='45/452498/Cv/5'>cysteine residue</scene> (C134 in ''Vibrio Cholerae'') which binds to inhibitors. The C terminal contains the homodimer intersubunit contacts. <ref>PMID:12493825</ref>
</StructureSection>
</StructureSection>
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**[[4r5m]] - VcASADH I + NADP + inhibitor<br />
**[[4r5m]] - VcASADH I + NADP + inhibitor<br />
}}
}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 14:38, 10 November 2015

Aspartate-semialdehyde dehydrogenase complex with NADP and substrate analog (PDB code 1mb4)

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3D Structures of Aspartate-semialdehyde dehydrogenase

Updated on 10-November-2015

References

  1. Blanco J, Moore RA, Kabaleeswaran V, Viola RE. A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae. Protein Sci. 2003 Jan;12(1):27-33. PMID:12493825

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Michal Harel, Alexander Berchansky

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