1xrm: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{STRUCTURE_1xrm| PDB=1xrm | SCENE= }} | {{STRUCTURE_1xrm| PDB=1xrm | SCENE= }} | ||
===Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe=== | ===Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe=== | ||
{{ABSTRACT_PUBMED_15994304}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC]] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids. | |||
==About this Structure== | ==About this Structure== | ||
[[1xrm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | [[1xrm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRM OCA]. | ||
==See Also== | ==See Also== | ||
| Line 14: | Line 13: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:015994304</ref><references group="xtra"/> | <ref group="xtra">PMID:015994304</ref><references group="xtra"/><references/> | ||
[[Category: Prolyl aminopeptidase]] | [[Category: Prolyl aminopeptidase]] | ||
[[Category: Brandstetter, H.]] | [[Category: Brandstetter, H.]] | ||
[[Category: Goehring, W.]] | [[Category: Goehring, W.]] | ||
