3unx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:03, 14 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3unx' size='340' side='right'caption='[[3unx]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
<StructureSection load='3unx' size='340' side='right'caption='[[3unx]], [[Resolution|resolution]] 1.26&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3unx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"denitrobacillus_licheniformis"_(weigmann_1898)_verhoeven_1952 "denitrobacillus licheniformis" (weigmann 1898) verhoeven 1952]. 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>
+
<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='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>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.26&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3unr|3unr]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apr ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1402 "Denitrobacillus licheniformis" (Weigmann 1898) Verhoeven 1952])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </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=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'>[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>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/SUBT_BACLI SUBT_BACLI]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
+
[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>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
A bond-distance analysis has been undertaken to determine the protonation states of ionizable amino acids in trypsin, subtilisin and lysozyme. The diffraction resolutions were 1.2 A for trypsin (97% complete, 12% H-atom visibility at 2.5sigma), 1.26 A for subtilisin (100% complete, 11% H-atom visibility at 2.5sigma) and 0.65 A for lysozyme (PDB entry 2vb1; 98% complete, 30% H-atom visibility at 3sigma). These studies provide a wide diffraction resolution range for assessment. The bond-length e.s.d.s obtained are as small as 0.008 A and thus provide an exceptional opportunity for bond-length analyses. The results indicate that useful information can be obtained from diffraction data at around 1.2-1.3 A resolution and that minor increases in resolution can have significant effects on reducing the associated bond-length standard deviations. The protonation states in histidine residues were also considered; however, owing to the smaller differences between the protonated and deprotonated forms it is much more difficult to infer the protonation states of these residues. Not even the 0.65 A resolution lysozyme structure provided the necessary accuracy to determine the protonation states of histidine.
+
-
 
+
-
Protonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completeness.,Fisher SJ, Blakeley MP, Cianci M, McSweeney S, Helliwell JR Acta Crystallogr D Biol Crystallogr. 2012 Jul;68(Pt 7):800-9. doi:, 10.1107/S0907444912012589. Epub 2012 Jun 15. PMID:22751665<ref>PMID:22751665</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3unx" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
Line 28: Line 17:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
 +
[[Category: Bacillus licheniformis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Subtilisin]]
+
[[Category: Blakeley MP]]
-
[[Category: Blakeley, M P]]
+
[[Category: Cianci M]]
-
[[Category: Cianci, M]]
+
[[Category: Fisher SJ]]
-
[[Category: Fisher, S J]]
+
[[Category: Helliwell JR]]
-
[[Category: Helliwell, J R]]
+
[[Category: McSweeny S]]
-
[[Category: McSweeny, S]]
+
-
[[Category: Hydrolase]]
+

Current revision

Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A resolution

PDB ID 3unx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3unx"
Personal tools