3sut: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:


==Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc==
==Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc==
<StructureSection load='3sut' size='340' side='right' caption='[[3sut]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3sut' size='340' side='right'caption='[[3sut]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3sut]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Paenibacillus_sp._ts12 Paenibacillus sp. ts12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SUT FirstGlance]. <br>
<table><tr><td colspan='2'>[[3sut]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_sp._ts12 Paenibacillus sp. ts12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SUT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OAN:O-(2-ACETAMIDO-2-DEOXY+D-GLUCOPYRANOSYLIDENE)+AMINO-N-PHENYLCARBAMATE'>OAN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OAN:O-(2-ACETAMIDO-2-DEOXY+D-GLUCOPYRANOSYLIDENE)+AMINO-N-PHENYLCARBAMATE'>OAN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sur|3sur]], [[3sus|3sus]], [[3suu|3suu]], [[3suv|3suv]], [[3suw|3suw]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sur|3sur]], [[3sus|3sus]], [[3suu|3suu]], [[3suv|3suv]], [[3suw|3suw]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hex1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192895 Paenibacillus sp. TS12])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hex1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=192895 Paenibacillus sp. TS12])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sut OCA], [http://pdbe.org/3sut PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3sut RCSB], [http://www.ebi.ac.uk/pdbsum/3sut PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3sut 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=3sut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sut OCA], [https://pdbe.org/3sut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sut RCSB], [https://www.ebi.ac.uk/pdbsum/3sut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sut ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
Line 22: Line 22:
==See Also==
==See Also==
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]]
*[[Beta-Hexosaminidase 3D structures|Beta-Hexosaminidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
Line 27: Line 28:
</StructureSection>
</StructureSection>
[[Category: Beta-N-acetylhexosaminidase]]
[[Category: Beta-N-acetylhexosaminidase]]
[[Category: Large Structures]]
[[Category: Paenibacillus sp. ts12]]
[[Category: Paenibacillus sp. ts12]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

Revision as of 11:11, 29 June 2022

Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAcCrystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc

Structural highlights

3sut is a 1 chain structure with sequence from Paenibacillus sp. ts12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:Hex1 (Paenibacillus sp. TS12)
Activity:Beta-N-acetylhexosaminidase, with EC number 3.2.1.52
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

One useful methodology that has been used to give insight into how chemically synthesized inhibitors bind to enzymes and the reasons underlying their potency is crystallographic studies of inhibitor-enzyme complexes. Presented here is the X-ray structural analysis of a representative family 20 exo-beta-N-acetylhexosaminidase in complex with various known classes of inhibitor of these types of enzymes, which highlights how different inhibitor classes can inhibit the same enzyme. This study will aid in the future development of inhibitors of not only exo-beta-N-acetylhexosaminidases but also other types of glycoside hydrolases.

Gaining insight into the inhibition of glycoside hydrolase family 20 exo-beta-N-acetylhexosaminidases using a structural approach.,Sumida T, Stubbs KA, Ito M, Yokoyama S Org Biomol Chem. 2012 Apr 7;10(13):2607-12. Epub 2012 Feb 27. PMID:22367352[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Sumida T, Stubbs KA, Ito M, Yokoyama S. Gaining insight into the inhibition of glycoside hydrolase family 20 exo-beta-N-acetylhexosaminidases using a structural approach. Org Biomol Chem. 2012 Apr 7;10(13):2607-12. Epub 2012 Feb 27. PMID:22367352 doi:10.1039/c2ob06636j

3sut, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA