4icr: Difference between revisions
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==Structural basis for substrate recognition and reaction mechanism of bacterial aminopeptidase peps== | |||
<StructureSection load='4icr' size='340' side='right'caption='[[4icr]], [[Resolution|resolution]] 2.17Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4icr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ICR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ICR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.17Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4icr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4icr OCA], [https://pdbe.org/4icr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4icr RCSB], [https://www.ebi.ac.uk/pdbsum/4icr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4icr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0H2UN95_STRPN A0A0H2UN95_STRPN] | |||
==See Also== | |||
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus pneumoniae TIGR4]] | |||
[[Category: Kim KK]] | |||
[[Category: Lee S]] | |||
[[Category: Ta MH]] | |||
Latest revision as of 11:53, 1 March 2024
Structural basis for substrate recognition and reaction mechanism of bacterial aminopeptidase peps
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