1gbh: Difference between revisions
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[[Image:1gbh.png|left|200px]] | [[Image:1gbh.png|left|200px]] | ||
{{STRUCTURE_1gbh| PDB=1gbh | SCENE= }} | {{STRUCTURE_1gbh| PDB=1gbh | SCENE= }} | ||
===ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID=== | ===ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID=== | ||
{{ABSTRACT_PUBMED_7500345}} | {{ABSTRACT_PUBMED_7500345}} | ||
==About this Structure== | ==About this Structure== | ||
[[1gbh]] 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=1GBH OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <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]] | ||
[[Category: | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
[[Category: Serine proteinase]] | |||
Revision as of 18:40, 21 November 2012
ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACIDALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY LEU COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-LEUCINE BORONIC ACID
Template:ABSTRACT PUBMED 7500345
About this StructureAbout this Structure
1gbh is a 2 chain structure with sequence from Lysobacter enzymogenes. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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