4xn5: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xn5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XN5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xn5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XN5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XN5 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.66Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</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=4xn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xn5 OCA], [https://pdbe.org/4xn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xn5 RCSB], [https://www.ebi.ac.uk/pdbsum/4xn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xn5 ProSAT]</span></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=4xn5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xn5 OCA], [https://pdbe.org/4xn5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xn5 RCSB], [https://www.ebi.ac.uk/pdbsum/4xn5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xn5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 18:29, 8 November 2023
Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-PhenylalanineCrystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-Phenylalanine
Structural highlights
FunctionAMPN_ECOLI Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. See Also |
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