4hpx: Difference between revisions
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{{STRUCTURE_4hpx| PDB=4hpx | SCENE= }} | |||
===Crystal structure of Tryptophan Synthase at 1.65 A resolution in complex with alpha aminoacrylate E(A-A) and benzimidazole in the beta site and the F9 inhibitor in the alpha site=== | |||
The | ==Function== | ||
[[http://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY]] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [[http://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | |||
==About this Structure== | |||
[[4hpx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HPX OCA]. | |||
[[Category: Tryptophan synthase]] | |||
[[Category: Dunn, M F.]] | |||
[[Category: Fan, L.]] | |||
[[Category: Hilario, E.]] | |||
[[Category: Mueller, L J.]] | |||
[[Category: Niks, D.]] | |||
[[Category: Allosteric enzyme]] | |||
[[Category: Alpha amino acrylate]] | |||
[[Category: Amino-acid biosynthesis]] | |||
[[Category: Aromatic amino acid biosynthesis]] | |||
[[Category: Benzimidazole]] | |||
[[Category: Carbon-oxygen lyase]] | |||
[[Category: F9f]] | |||
[[Category: Lyase]] | |||
[[Category: Lyase-lyase inhibitor complex]] | |||
[[Category: Pyridoxal phosphate]] | |||
[[Category: Salmonella]] | |||
[[Category: Tryptophan biosynthesis]] | |||
Revision as of 10:35, 18 December 2013
Crystal structure of Tryptophan Synthase at 1.65 A resolution in complex with alpha aminoacrylate E(A-A) and benzimidazole in the beta site and the F9 inhibitor in the alpha site
Function
[TRPA_SALTY] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. [TRPB_SALTY] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
About this Structure
4hpx is a 2 chain structure. Full crystallographic information is available from OCA.
