3iap

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[[Image:3iap.png|left|200px]]
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{{STRUCTURE_3iap| PDB=3iap | SCENE= }}
{{STRUCTURE_3iap| PDB=3iap | SCENE= }}
===E. coli (lacZ) beta-galactosidase (E416Q)===
===E. coli (lacZ) beta-galactosidase (E416Q)===
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{{ABSTRACT_PUBMED_19936901}}
{{ABSTRACT_PUBMED_19936901}}
==About this Structure==
==About this Structure==
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3IAP is a 4 chains structure with sequences from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IAP OCA].
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[[3iap]] is a 4 chain structure of [[Galactosidase]] with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IAP OCA].
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==See Also==
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*[[Galactosidase|Galactosidase]]
==Reference==
==Reference==
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<ref group="xtra">PMID:19936901</ref><references group="xtra"/>
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<ref group="xtra">PMID:019936901</ref><references group="xtra"/>
[[Category: Beta-galactosidase]]
[[Category: Beta-galactosidase]]
[[Category: Escherichia coli k-12]]
[[Category: Escherichia coli k-12]]
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[[Category: Glycosidase]]
[[Category: Glycosidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 17:54, 26 July 2012


PDB ID 3iap

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3iap, resolution 2.00Å ()
Ligands: , , ,
Gene: lacZ (Escherichia coli K-12)
Activity: Beta-galactosidase, with EC number 3.2.1.23
Related: 1dp0, 3dym, 3iaq
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Contents

E. coli (lacZ) beta-galactosidase (E416Q)

Template:ABSTRACT PUBMED 19936901

About this Structure

3iap is a 4 chain structure of Galactosidase with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.

See Also

Reference

  • Lo S, Dugdale ML, Jeerh N, Ku T, Roth NJ, Huber RE. Studies of Glu-416 Variants of beta-Galactosidase (E. coli) Show that the Active Site Mg(2+) is Not Important for Structure and Indicate that the Main Role of Mg (2+) is to Mediate Optimization of Active Site Chemistry. Protein J. 2009 Nov 21. PMID:19936901 doi:10.1007/s10930-009-9216-x

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