3f49: Difference between revisions

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==Anion-triggered Engineered Subtilisin SUBT_BACAM==
==Anion-triggered Engineered Subtilisin SUBT_BACAM==
<StructureSection load='3f49' size='340' side='right' caption='[[3f49]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='3f49' size='340' side='right'caption='[[3f49]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3f49]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F49 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F49 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3f49]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F49 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F49 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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, SUBT_BACAM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">apr, SUBT_BACAM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1390 "Bacillus amyloliquifaciens" (sic) Fukumoto 1943])</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='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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f49 OCA], [http://pdbe.org/3f49 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f49 RCSB], [http://www.ebi.ac.uk/pdbsum/3f49 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f49 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=3f49 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f49 OCA], [https://pdbe.org/3f49 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f49 RCSB], [https://www.ebi.ac.uk/pdbsum/3f49 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f49 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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>   
[[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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==See Also==
==See Also==
*[[Subtilisin|Subtilisin]]
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Subtilisin]]
[[Category: Subtilisin]]
[[Category: Bryan, P N]]
[[Category: Bryan, P N]]

Revision as of 22:49, 20 October 2021

Anion-triggered Engineered Subtilisin SUBT_BACAMAnion-triggered Engineered Subtilisin SUBT_BACAM

Structural highlights

3f49 is a 1 chain structure with sequence from "bacillus_amyloliquifaciens"_(sic)_fukumoto_1943 "bacillus amyloliquifaciens" (sic) fukumoto 1943. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:apr, SUBT_BACAM ("Bacillus amyloliquifaciens" (sic) Fukumoto 1943)
Activity:Subtilisin, with EC number 3.4.21.62
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Peng Y, Huang Q, Zhang RH, Zhang YZ. Purification and characterization of a fibrinolytic enzyme produced by Bacillus amyloliquefaciens DC-4 screened from douchi, a traditional Chinese soybean food. Comp Biochem Physiol B Biochem Mol Biol. 2003 Jan;134(1):45-52. PMID:12524032

3f49, resolution 1.70Å

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