7qjr

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7qjr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QJR FirstGlance]. <br>
<table><tr><td colspan='2'>[[7qjr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca Thermobifida fusca]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QJR 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=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 1.51&#8491;</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=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=7qjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qjr OCA], [https://pdbe.org/7qjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qjr RCSB], [https://www.ebi.ac.uk/pdbsum/7qjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qjr 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=7qjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qjr OCA], [https://pdbe.org/7qjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qjr RCSB], [https://www.ebi.ac.uk/pdbsum/7qjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qjr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (Ref.4, PubMed:31690819, PubMed:24728714, PubMed:23604968, PubMed:15638529, PubMed:25545638). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (Ref.4, PubMed:25545638, PubMed:31690819, PubMed:32269349). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).<ref>PMID:15638529</ref> <ref>PMID:20816933</ref> <ref>PMID:23604968</ref> <ref>PMID:24728714</ref> <ref>PMID:25545638</ref> <ref>PMID:31690819</ref> <ref>PMID:32269349</ref> <ref>PMID:20816933</ref>
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[https://www.uniprot.org/uniprot/PETH2_THEFU PETH2_THEFU] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:23604968, PubMed:24728714, PubMed:31690819, Ref.4). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:15638529, PubMed:23604968, PubMed:24728714, PubMed:25545638, PubMed:31690819, Ref.4). Also hydrolyzes the triglycerides triacetin, tributyrin, tricaprin, and trilaurin, with a preference for short-chain substrates (PubMed:15638529). Hydrolyzes the hemicellulose xylan (PubMed:20816933). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638, PubMed:31690819, PubMed:32269349, Ref.4). Can also depolymerize poly(epsilon-caprolactone) (PCL), a synthetic aliphatic biodegradable polyester (PubMed:15638529). Hydrolyzes polyoxyethylenesorbate esters with a preference for shorter chain lengths (PubMed:20816933).<ref>PMID:15638529</ref> <ref>PMID:20816933</ref> <ref>PMID:23604968</ref> <ref>PMID:24728714</ref> <ref>PMID:25545638</ref> <ref>PMID:31690819</ref> <ref>PMID:32269349</ref> <ref>PMID:20816933</ref>
== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of cutinase 1 from Thermobifida fusca DSM44342 (703)

PDB ID 7qjr

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