2yq8
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yq8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yq8 RCSB], [http://www.ebi.ac.uk/pdbsum/2yq8 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yq8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yq8 RCSB], [http://www.ebi.ac.uk/pdbsum/2yq8 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/P4HA1_HUMAN P4HA1_HUMAN]] Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 04:22, 25 December 2014
Crystal structure of the SeMet-labeled N-terminal domain and peptide substrate binding domain of alpha subunit of prolyl-4 hydroxylase type I from human.
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