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4jjf

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m (Protected "4jjf" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4jjf| PDB=4jjf | SCENE= }}
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===Crystal structure of FE-hydrogenase from methanothermobacter marburgensis in complex with 2-naphthylisocyanide===
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{{ABSTRACT_PUBMED_23873755}}
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The entry 4jjf is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/HMD_METTM HMD_METTM]] Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.
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Authors: Tamura, H., Warkentin, E., Ermler, U., Shima, S.
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==About this Structure==
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[[4jjf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_marburgensis Methanothermobacter marburgensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JJF OCA].
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Description: Crystal structure of FE-hydrogenase from methanothermobacter marburgensis in complex with 2-naphthylisocyanide
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==Reference==
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<ref group="xtra">PMID:023873755</ref><references group="xtra"/><references/>
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[[Category: 5,10-methenyltetrahydromethanopterin hydrogenase]]
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[[Category: Methanothermobacter marburgensis]]
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[[Category: Ermler, U.]]
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[[Category: Shima, S.]]
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[[Category: Tamura, H.]]
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[[Category: Warkentin, E.]]
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[[Category: Alpha-beta fold]]
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[[Category: Hydrogenase]]
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[[Category: Oxidoreductase]]

Revision as of 20:55, 7 August 2013

Template:STRUCTURE 4jjf

Contents

Crystal structure of FE-hydrogenase from methanothermobacter marburgensis in complex with 2-naphthylisocyanide

Template:ABSTRACT PUBMED 23873755

Function

[HMD_METTM] Catalyzes the reversible reduction of methenyl-H(4)MPT(+) to methylene-H(4)MPT.

About this Structure

4jjf is a 2 chain structure with sequence from Methanothermobacter marburgensis. Full crystallographic information is available from OCA.

Reference

  • Tamura H, Salomone-Stagni M, Fujishiro T, Warkentin E, Meyer-Klaucke W, Ermler U, Shima S. Crystal Structures of [Fe]-Hydrogenase in Complex with Inhibitory Isocyanides: Implications for the H -Activation Site. Angew Chem Int Ed Engl. 2013 Jul 22. doi: 10.1002/anie.201305089. PMID:23873755 doi:10.1002/anie.201305089

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OCA

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