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3unx
From Proteopedia
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==Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A resolution== | ==Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A resolution== | ||
| - | <StructureSection load='3unx' size='340' side='right' caption='[[3unx]], [[Resolution|resolution]] 1.26Å' scene=''> | + | <StructureSection load='3unx' size='340' side='right'caption='[[3unx]], [[Resolution|resolution]] 1.26Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3unx]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3unx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UNX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UNX FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.26Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3unx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3unx OCA], [https://pdbe.org/3unx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3unx RCSB], [https://www.ebi.ac.uk/pdbsum/3unx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3unx ProSAT]</span></td></tr> |
| - | < | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| - | + | == Function == | |
| - | = | + | [https://www.uniprot.org/uniprot/SUBC_BACLI SUBC_BACLI] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides (Ref.4, PubMed:11109488). Shows high specificity for aromatic and hydrophobic amino acids in the P1 substrate position (PubMed:11109488). May play an important role in the degradation of feather keratin (PubMed:11109488).<ref>PMID:11109488</ref> <ref>PMID:4967581</ref> |
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| - | </ | + | |
==See Also== | ==See Also== | ||
| - | *[[Subtilisin|Subtilisin]] | + | *[[Subtilisin 3D structures|Subtilisin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Blakeley | + | [[Category: Blakeley MP]] |
| - | [[Category: Cianci | + | [[Category: Cianci M]] |
| - | [[Category: Fisher | + | [[Category: Fisher SJ]] |
| - | [[Category: Helliwell | + | [[Category: Helliwell JR]] |
| - | [[Category: McSweeny | + | [[Category: McSweeny S]] |
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Current revision
Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A resolution
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