2dp4: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<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 ==
<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>
<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>
</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>
</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>
<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>
<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 ==
[[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> 
[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]]
Line 15: Line 14:
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/2dp4_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dp/2dp4_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
Line 22: Line 21:


==See Also==
==See Also==
*[[Proteinase|Proteinase]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Engyodontium album]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptidase K]]
[[Category: Parengyodontium album]]
[[Category: Bhushan, A]]
[[Category: Bhushan A]]
[[Category: Sharma, S]]
[[Category: Sharma S]]
[[Category: Singh, A K]]
[[Category: Singh AK]]
[[Category: Singh, N]]
[[Category: Singh N]]
[[Category: Singh, T P]]
[[Category: Singh TP]]
[[Category: Hydrolase]]
[[Category: Lactoferrin fragment]]
[[Category: Proteinase k]]

Latest revision as of 12:05, 6 November 2024

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

Structural highlights

2dp4 is a 2 chain structure with sequence from Homo sapiens and Parengyodontium album. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.9Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRTK_PARAQ Hydrolyzes keratin at aromatic and hydrophobic residues.

Evolutionary Conservation

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

See Also

2dp4, resolution 2.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2dp4&oldid=4196489"