2yd0: Difference between revisions

<StructureSection load='2yd0' size='340' side='right'caption='[[2yd0]], [[Resolution|resolution]] 2.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[2yd0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2xdt 2xdt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YD0 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]] 2.7&#8491;</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BES:2-(3-AMINO-2-HYDROXY-4-PHENYL-BUTYRYLAMINO)-4-METHYL-PENTANOIC+ACID'>BES</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=2yd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yd0 OCA], [https://pdbe.org/2yd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yd0 RCSB], [https://www.ebi.ac.uk/pdbsum/2yd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yd0 ProSAT]</span></td></tr>

[https://www.uniprot.org/uniprot/ERAP1_HUMAN ERAP1_HUMAN] Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.<ref>PMID:15908954</ref> <ref>PMID:16286653</ref> <ref>PMID:21478864</ref>  

*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Allerston C]]

[[Category: Arrowsmith CH]]

[[Category: Bountra C]]

[[Category: Chaikuad A]]

[[Category: Edwards A]]

[[Category: Knapp S]]

[[Category: Kochan G]]

[[Category: Krojer T]]

[[Category: Muniz JRC]]

[[Category: Raynor J]]

[[Category: Ugochukwu E]]

[[Category: Vollmar M]]

[[Category: Weigelt J]]

[[Category: Von Delft F]]