4h2k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 9: Line 9:
<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=4h2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h2k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h2k RCSB], [http://www.ebi.ac.uk/pdbsum/4h2k 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=4h2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h2k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4h2k RCSB], [http://www.ebi.ac.uk/pdbsum/4h2k PDBsum]</span></td></tr>
</table>
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/DAPE_HAEIN DAPE_HAEIN]] Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. It can only hydrolyze L,L-N-succinyl-diaminopimelic acid (L,L-SDAP) and is inactive toward D,L-, L,D-, and D,D-SDAP.<ref>PMID:12962500</ref> <ref>PMID:16421726</ref> <ref>PMID:18712420</ref>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 08:43, 24 December 2014

Crystal structure of the catalytic domain of succinyl-diaminopimelate desuccinylase from Haemophilus influenzae

4h2k, resolution 1.84Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools