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2dp4

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Current revision (08:27, 25 October 2023) (edit) (undo)
 
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<StructureSection load='2dp4' size='340' side='right'caption='[[2dp4]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='2dp4' size='340' side='right'caption='[[2dp4]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2dp4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DP4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2dp4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Parengyodontium_album Parengyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DP4 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3prk|3prk]], [[1bjr|1bjr]]</div></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]] 2.9&#8491;</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/Peptidase_K Peptidase K], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </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=2dp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dp4 OCA], [https://pdbe.org/2dp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dp4 RCSB], [https://www.ebi.ac.uk/pdbsum/2dp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dp4 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=2dp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dp4 OCA], [https://pdbe.org/2dp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dp4 RCSB], [https://www.ebi.ac.uk/pdbsum/2dp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dp4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PRTK_TRIAL PRTK_TRIAL]] Hydrolyzes keratin at aromatic and hydrophobic residues. [[https://www.uniprot.org/uniprot/TRFL_HUMAN TRFL_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Lactotransferrin has antimicrobial activity which depends on the extracellular cation concentration.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref> Isoform DeltaLf: transcription factor with antiproliferative properties and inducing cell cycle arrest. Binds to DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.<ref>PMID:12535064</ref> <ref>PMID:22320386</ref>
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[https://www.uniprot.org/uniprot/PRTK_PARAQ PRTK_PARAQ] Hydrolyzes keratin at aromatic and hydrophobic residues.
== 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==
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*[[Proteinase|Proteinase]]
 
*[[Proteinase 3D structures|Proteinase 3D structures]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Engyodontium album]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidase K]]
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[[Category: Parengyodontium album]]
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[[Category: Bhushan, A]]
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[[Category: Bhushan A]]
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[[Category: Sharma, S]]
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[[Category: Sharma S]]
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[[Category: Singh, A K]]
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[[Category: Singh AK]]
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[[Category: Singh, N]]
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[[Category: Singh N]]
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[[Category: Singh, T P]]
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[[Category: Singh TP]]
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[[Category: Hydrolase]]
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[[Category: Lactoferrin fragment]]
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[[Category: Proteinase k]]
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Current revision

Crystal structure of the complex formed between proteinase K and a human lactoferrin fragment at 2.9 A resolution

PDB ID 2dp4

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