1lam: Difference between revisions
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[[Image:1lam.png|left|200px]] | [[Image:1lam.png|left|200px]] | ||
{{STRUCTURE_1lam| PDB=1lam | SCENE= }} | {{STRUCTURE_1lam| PDB=1lam | SCENE= }} | ||
===LEUCINE AMINOPEPTIDASE (UNLIGATED)=== | ===LEUCINE AMINOPEPTIDASE (UNLIGATED)=== | ||
{{ABSTRACT_PUBMED_7578088}} | {{ABSTRACT_PUBMED_7578088}} | ||
==About this Structure== | ==About this Structure== | ||
[[1lam]] is a 1 chain structure of [[Aminopeptidase]] with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAM OCA]. | |||
==See Also== | |||
*[[Aminopeptidase|Aminopeptidase]] | |||
*[[Metalloproteases|Metalloproteases]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:007578088</ref><ref group="xtra">PMID:011604529</ref><ref group="xtra">PMID:011917145</ref><references group="xtra"/> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Leucyl aminopeptidase]] | [[Category: Leucyl aminopeptidase]] | ||
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[[Category: Exopeptidase]] | [[Category: Exopeptidase]] | ||
[[Category: Metallopeptidase]] | [[Category: Metallopeptidase]] | ||
Revision as of 21:45, 26 July 2012
LEUCINE AMINOPEPTIDASE (UNLIGATED)LEUCINE AMINOPEPTIDASE (UNLIGATED)
Template:ABSTRACT PUBMED 7578088
About this StructureAbout this Structure
1lam is a 1 chain structure of Aminopeptidase with sequence from Bos taurus. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Strater N, Lipscomb WN. Two-metal ion mechanism of bovine lens leucine aminopeptidase: active site solvent structure and binding mode of L-leucinal, a gem-diolate transition state analogue, by X-ray crystallography. Biochemistry. 1995 Nov 14;34(45):14792-800. PMID:7578088
- ↑ Hayward S. Peptide-plane flipping in proteins. Protein Sci. 2001 Nov;10(11):2219-27. PMID:11604529 doi:10.1110/ps.23101
- ↑ Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145