1xro: Difference between revisions
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[[Image:1xro.png|left|200px]] | [[Image:1xro.png|left|200px]] | ||
{{STRUCTURE_1xro| PDB=1xro | SCENE= }} | {{STRUCTURE_1xro| PDB=1xro | SCENE= }} | ||
===Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu=== | ===Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu=== | ||
{{ABSTRACT_PUBMED_15994304}} | {{ABSTRACT_PUBMED_15994304}} | ||
==About this Structure== | ==About this Structure== | ||
[[1xro]] is a 1 chain structure of [[Aminopeptidase]] with sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRO OCA]. | |||
==See Also== | |||
*[[Aminopeptidase|Aminopeptidase]] | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:015994304</ref><references group="xtra"/> | ||
[[Category: Prolyl aminopeptidase]] | [[Category: Prolyl aminopeptidase]] | ||
[[Category: Thermoplasma acidophilum]] | [[Category: Thermoplasma acidophilum]] | ||
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[[Category: Caged active site]] | [[Category: Caged active site]] | ||
[[Category: Hydrogen bonded network]] | [[Category: Hydrogen bonded network]] | ||
[[Category: Hydrolase]] | |||
[[Category: Peptide cleavage]] | [[Category: Peptide cleavage]] | ||
[[Category: Substrate recognition]] | [[Category: Substrate recognition]] | ||
Revision as of 08:35, 27 July 2012
Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu
Template:ABSTRACT PUBMED 15994304
About this Structure
1xro is a 1 chain structure of Aminopeptidase with sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.
See Also
Reference
- Goettig P, Brandstetter H, Groll M, Gohring W, Konarev PV, Svergun DI, Huber R, Kim JS. X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum. J Biol Chem. 2005 Sep 30;280(39):33387-96. Epub 2005 Jul 1. PMID:15994304 doi:https://dx.doi.org/10.1074/jbc.M505030200
