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==Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase==
==Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase==
<StructureSection load='5arb' size='340' side='right' caption='[[5arb]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
<StructureSection load='5arb' size='340' side='right'caption='[[5arb]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5arb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ARB FirstGlance]. <br>
<table><tr><td colspan='2'>[[5arb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ARB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EI3:5-METHYL-2-(5-METHYLPYRIDIN-2-YL)PYRIDINE'>EI3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5aqe|5aqe]], [[5arc|5arc]], [[5ard|5ard]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EI3:5-METHYL-2-(5-METHYLPYRIDIN-2-YL)PYRIDINE'>EI3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://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=5arb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5arb OCA], [https://pdbe.org/5arb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5arb RCSB], [https://www.ebi.ac.uk/pdbsum/5arb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5arb ProSAT]</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=5arb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5arb OCA], [http://pdbe.org/5arb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5arb RCSB], [http://www.ebi.ac.uk/pdbsum/5arb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5arb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SUBS_BACLE SUBS_BACLE]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.  
[https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
 
==See Also==
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Subtilisin]]
[[Category: Large Structures]]
[[Category: Davies, G J]]
[[Category: Lederbergia lenta]]
[[Category: Davis, B G]]
[[Category: Davies GJ]]
[[Category: Diaz-Rodriguez, A]]
[[Category: Davis BG]]
[[Category: Mcdonough, M]]
[[Category: Diaz-Rodriguez A]]
[[Category: Offen, W A]]
[[Category: Mcdonough M]]
[[Category: Palm-Espling, M E]]
[[Category: Offen WA]]
[[Category: Pordea, A]]
[[Category: Palm-Espling ME]]
[[Category: Sharma, M]]
[[Category: Pordea A]]
[[Category: Wormald, M R]]
[[Category: Sharma M]]
[[Category: Catalysis]]
[[Category: Wormald MR]]
[[Category: Cross-coupling]]
[[Category: Heck reaction]]
[[Category: Hydrolase]]
[[Category: Metalloenzyme]]
[[Category: Palladium]]
[[Category: Protease]]

Latest revision as of 14:16, 10 January 2024

Cooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling HeckaseCooperative bio-metallic selectivity in a tailored protease enables creation of a C-C cross-coupling Heckase

Structural highlights

5arb is a 1 chain structure with sequence from Lederbergia lenta. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.15Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SUBS_LEDLE Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.

See Also

5arb, resolution 1.15Å

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