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3zei

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'''Unreleased structure'''
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{{STRUCTURE_3zei| PDB=3zei | SCENE= }}
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===Structure of the Mycobacterium tuberculosis O-Acetylserine Sulfhydrylase (OASS) CysK1 in complex with a small molecule inhibitor===
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{{ABSTRACT_PUBMED_23879381}}
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The entry 3zei is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/CYSK_MYCTU CYSK_MYCTU]] Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide.
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Authors: Poyraz, O., Schnell, R., Schneider, G.
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==About this Structure==
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[[3zei]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZEI OCA].
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Description: Structure of the Mycobacterium tuberculosis O-Acetylserine Sulfhydrylase (OASS) CysK1 in complex with a small molecule inhibitor
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==Reference==
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<ref group="xtra">PMID:023879381</ref><references group="xtra"/><references/>
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[[Category: Cysteine synthase]]
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[[Category: Mycobacterium tuberculosis]]
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[[Category: Poyraz, O.]]
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[[Category: Schneider, G.]]
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[[Category: Schnell, R.]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]

Revision as of 20:50, 7 August 2013

Template:STRUCTURE 3zei

Contents

Structure of the Mycobacterium tuberculosis O-Acetylserine Sulfhydrylase (OASS) CysK1 in complex with a small molecule inhibitor

Template:ABSTRACT PUBMED 23879381

Function

[CYSK_MYCTU] Catalyzes the conversion of O-acetylserine (OAS) to cysteine through the elimination of acetate and addition of hydrogen sulfide.

About this Structure

3zei is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

  • Poyraz O, Jeankumar VU, Saxena S, Schnell R, Haraldsson M, Yogeeswari P, Sriram D, Schneider G. Structure-Guided Design of Novel Thiazolidine Inhibitors of O-Acetyl Serine Sulfhydrylase from Mycobacterium tuberculosis. J Med Chem. 2013 Jul 23. PMID:23879381 doi:10.1021/jm400710k

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