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1to1

From Proteopedia

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Current revision (06:32, 23 August 2023) (edit) (undo)
 
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<StructureSection load='1to1' size='340' side='right'caption='[[1to1]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
<StructureSection load='1to1' size='340' side='right'caption='[[1to1]], [[Resolution|resolution]] 1.68&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1to1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943] and [https://en.wikipedia.org/wiki/Domesticated_barley Domesticated barley]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TO1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1to1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_amyloliquefaciens Bacillus amyloliquefaciens] and [https://en.wikipedia.org/wiki/Hordeum_vulgare_subsp._vulgare Hordeum vulgare subsp. vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TO1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1tm1|1tm1]], [[1tm3|1tm3]], [[1tm4|1tm4]], [[1tm5|1tm5]], [[1tm7|1tm7]], [[1tmg|1tmg]], [[1t02|1t02]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<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=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1to1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1to1 OCA], [https://pdbe.org/1to1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1to1 RCSB], [https://www.ebi.ac.uk/pdbsum/1to1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1to1 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=1to1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1to1 OCA], [https://pdbe.org/1to1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1to1 RCSB], [https://www.ebi.ac.uk/pdbsum/1to1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1to1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/SUBT_BACAM SUBT_BACAM]] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.<ref>PMID:12524032</ref>
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[https://www.uniprot.org/uniprot/SUBT_BACAM SUBT_BACAM] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. Has a high substrate specificity to fibrin.<ref>PMID:12524032</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Domesticated barley]]
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[[Category: Bacillus amyloliquefaciens]]
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[[Category: Hordeum vulgare subsp. vulgare]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Subtilisin]]
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[[Category: Karen Lu CJ]]
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[[Category: Koshland, D E]]
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[[Category: Koshland Jr DE]]
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[[Category: Kwan, G]]
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[[Category: Kwan G]]
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[[Category: Lu, C J.Karen]]
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[[Category: Radisky ES]]
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[[Category: Radisky, E S]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Serine protease]]
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Current revision

crystal structure of the complex of subtilisin BPN' with chymotrypsin inhibitor 2 Y61A mutant

PDB ID 1to1

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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