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1gbc

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[[Image:1gbc.png|left|200px]]
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{{STRUCTURE_1gbc| PDB=1gbc | SCENE= }}
{{STRUCTURE_1gbc| PDB=1gbc | SCENE= }}
===ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID===
===ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID===
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{{ABSTRACT_PUBMED_7500345}}
{{ABSTRACT_PUBMED_7500345}}
==About this Structure==
==About this Structure==
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1GBC is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBC OCA].
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[[1gbc]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GBC OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:7500345</ref><references group="xtra"/>
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<ref group="xtra">PMID:007500345</ref><references group="xtra"/>
[[Category: Alpha-lytic endopeptidase]]
[[Category: Alpha-lytic endopeptidase]]
[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
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[[Category: Mace, J E.]]
[[Category: Mace, J E.]]
[[Category: Active-site mutation]]
[[Category: Active-site mutation]]
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[[Category: Inhibitor complex]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Serine proteinase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 14:22:35 2009''
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Revision as of 15:33, 21 November 2012

Template:STRUCTURE 1gbc

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID

Template:ABSTRACT PUBMED 7500345

About this Structure

1gbc is a 2 chain structure with sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA.

Reference

  • Mace JE, Agard DA. Kinetic and structural characterization of mutations of glycine 216 in alpha-lytic protease: a new target for engineering substrate specificity. J Mol Biol. 1995 Dec 8;254(4):720-36. PMID:7500345 doi:http://dx.doi.org/10.1006/jmbi.1995.0650

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