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1ogx

From Proteopedia

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[[Image:1ogx.png|left|200px]]
 
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{{STRUCTURE_1ogx| PDB=1ogx | SCENE= }}
{{STRUCTURE_1ogx| PDB=1ogx | SCENE= }}
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===HIGH RESOLUTION CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE MUTANT D40N(D38N, TI NUMBERING) FROM PSEUDOMONAS PUTIDA COMPLEXED WITH EQUILENIN AT 2.0 A RESOLUTION.===
===HIGH RESOLUTION CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE MUTANT D40N(D38N, TI NUMBERING) FROM PSEUDOMONAS PUTIDA COMPLEXED WITH EQUILENIN AT 2.0 A RESOLUTION.===
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{{ABSTRACT_PUBMED_11007792}}
{{ABSTRACT_PUBMED_11007792}}
==About this Structure==
==About this Structure==
[[1ogx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e3n 1e3n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGX OCA].
[[1ogx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e3n 1e3n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OGX OCA].
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==See Also==
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*[[Ketosteroid Isomerase|Ketosteroid Isomerase]]
==Reference==
==Reference==

Revision as of 09:13, 11 March 2013

Template:STRUCTURE 1ogx

Contents

HIGH RESOLUTION CRYSTAL STRUCTURE OF KETOSTEROID ISOMERASE MUTANT D40N(D38N, TI NUMBERING) FROM PSEUDOMONAS PUTIDA COMPLEXED WITH EQUILENIN AT 2.0 A RESOLUTION.

Template:ABSTRACT PUBMED 11007792

About this Structure

1ogx is a 2 chain structure with sequence from Pseudomonas putida. This structure supersedes the now removed PDB entry 1e3n. Full crystallographic information is available from OCA.

See Also

Reference

  • Ha NC, Kim MS, Lee W, Choi KY, Oh BH. Detection of large pKa perturbations of an inhibitor and a catalytic group at an enzyme active site, a mechanistic basis for catalytic power of many enzymes. J Biol Chem. 2000 Dec 29;275(52):41100-6. PMID:11007792 doi:http://dx.doi.org/10.1074/jbc.M007561200

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