4op4: Difference between revisions

No edit summary
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{STRUCTURE_4op4|  PDB=4op4  |  SCENE=  }}
===Crystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound form===


==Function==
==Crystal structure of the catalytic domain of DapE protein from V.cholerea in the Zn bound form==
[[http://www.uniprot.org/uniprot/DAPE_VIBCH DAPE_VIBCH]] 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 (By similarity).[HAMAP-Rule:MF_01690]  
<StructureSection load='4op4' size='340' side='right'caption='[[4op4]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[4op4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3t6m 3t6m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OP4 FirstGlance]. <br>
[[4op4]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3t6m 3t6m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OP4 OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.651&#8491;</td></tr>
[[Category: Succinyl-diaminopimelate desuccinylase]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BU1:1,4-BUTANEDIOL'>BU1</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Anderson, W F.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4op4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4op4 OCA], [https://pdbe.org/4op4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4op4 RCSB], [https://www.ebi.ac.uk/pdbsum/4op4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4op4 ProSAT]</span></td></tr>
[[Category: CSGID, Center for Structural Genomics of Infectious Diseases.]]
</table>
[[Category: Jedrzejczak, R.]]
== Function ==
[[Category: Joachimiak, A.]]
[https://www.uniprot.org/uniprot/DAPE_VIBCH DAPE_VIBCH] 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 (By similarity).[HAMAP-Rule:MF_01690]
[[Category: Makowska-Grzyska, M.]]
__TOC__
[[Category: Nocek, B.]]
</StructureSection>
[[Category: Aminopeptidase]]
[[Category: Large Structures]]
[[Category: Center for structural genomics of infectious disease]]
[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
[[Category: Csgid]]
[[Category: Anderson WF]]
[[Category: Hydrolase]]
[[Category: Jedrzejczak R]]
[[Category: M20]]
[[Category: Joachimiak A]]
[[Category: National institute of allergy and infectious disease]]
[[Category: Makowska-Grzyska M]]
[[Category: Niaid]]
[[Category: Nocek B]]
[[Category: Structural genomic]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA