This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3m1h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (16:28, 1 November 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal Structure Analysis of the K3 Cleaved Adhesin Domain of Lys-gingipain (Kgp) from Porphyromonas gingivalis w83==
==Crystal Structure Analysis of the K3 Cleaved Adhesin Domain of Lys-gingipain (Kgp) from Porphyromonas gingivalis w83==
-
<StructureSection load='3m1h' size='340' side='right' caption='[[3m1h]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
+
<StructureSection load='3m1h' size='340' side='right'caption='[[3m1h]], [[Resolution|resolution]] 1.56&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3m1h]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Porgi Porgi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M1H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M1H FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3m1h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis_W83 Porphyromonas gingivalis W83]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M1H FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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]] 1.56&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3km5|3km5]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">kgp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=242619 PORGI])</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=3m1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m1h OCA], [https://pdbe.org/3m1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m1h RCSB], [https://www.ebi.ac.uk/pdbsum/3m1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m1h ProSAT]</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=3m1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m1h OCA], [http://pdbe.org/3m1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m1h RCSB], [http://www.ebi.ac.uk/pdbsum/3m1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m1h ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/KGP83_PORGN KGP83_PORGN]] Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria (By similarity).[UniProtKB:B2RLK2]
+
[https://www.uniprot.org/uniprot/KGP83_PORGN KGP83_PORGN] Cysteine proteinase with a strong preference for substrates with Lys in the P1 position. Hydrolyzes bovine hemoglobin, bovine serum albumin, casein, human placental type I collagen and human IgA and IgG. Disrupts the functions of polymorphonuclear leukocytes. May act as a virulence factor in the development of peridontal disease. Involved in the coaggregation of P.gingivalis with other oral bacteria (By similarity).[UniProtKB:B2RLK2]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 20: Line 19:
</div>
</div>
<div class="pdbe-citations 3m1h" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3m1h" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Proteinase 3D structures|Proteinase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Porgi]]
+
[[Category: Large Structures]]
-
[[Category: Collyer, C A]]
+
[[Category: Porphyromonas gingivalis W83]]
-
[[Category: Hunter, N]]
+
[[Category: Collyer CA]]
-
[[Category: Li, N]]
+
[[Category: Hunter N]]
-
[[Category: Beta jelly roll barrel]]
+
[[Category: Li N]]
-
[[Category: Carbohydrate binding]]
+
-
[[Category: Cell invasion]]
+
-
[[Category: Cleaved adhesin family]]
+
-
[[Category: Hemagglutination domain]]
+
-
[[Category: Lys-gingipain]]
+
-
[[Category: Protease]]
+

Current revision

Crystal Structure Analysis of the K3 Cleaved Adhesin Domain of Lys-gingipain (Kgp) from Porphyromonas gingivalis w83

PDB ID 3m1h

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3m1h"
Personal tools