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4bt8

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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=4bt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bt8 RCSB], [http://www.ebi.ac.uk/pdbsum/4bt8 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=4bt8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bt8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bt8 RCSB], [http://www.ebi.ac.uk/pdbsum/4bt8 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[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.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 20:35, 25 December 2014

CRYSTAL STRUCTURE OF THE APO FORM OF N-TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE TYPE I FROM HUMAN

4bt8, resolution 2.20Å

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