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.

3dyb

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:58, 25 October 2017

proteinase K- digalacturonic acid complex

Structural highlights

3dyb is a 1 chain structure with sequence from Engyodontium album. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Activity:	Peptidase K, with EC number 3.4.21.64
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PRTK_TRIAL] 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.

Publication Abstract from PubMed

Proteinase K, a subtilisin-like fungal protease, was crystallized from a cocktail of small molecules containing digalacturonic acid (DGA). The crystal structure was determined to 1.32 A resolution and refined to an R factor of 0.158. The final model contained, beside the protein, two calcium ions, 379 water molecules, a molecule of DGA and a partially occupied HEPES molecule. The DGA molecule has one sugar moiety disposed exactly on a crystallographic twofold axis; the second ring was not observed. The DGA molecule is bound to two protein molecules across the twofold axis through hydrogen-bonding networks involving Ser150 and water molecules. One of the calcium-ion sites has not been reported previously. This study further illustrates the involvement of small molecules in the crystallization of macromolecules through their ability to form intermolecular lattice interactions.

High-resolution structure of proteinase K cocrystallized with digalacturonic acid.,Larson SB, Day JS, Nguyen C, Cudney R, McPherson A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt, 3):192-8. Epub 2009 Feb 12. PMID:19255463^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Larson SB, Day JS, Nguyen C, Cudney R, McPherson A. High-resolution structure of proteinase K cocrystallized with digalacturonic acid. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt, 3):192-8. Epub 2009 Feb 12. PMID:19255463 doi:10.1107/S1744309109002218

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dyb"

@@ Line 1: / Line 1: @@
 ==proteinase K- digalacturonic acid complex==
 <StructureSection load='3dyb' size='340' side='right' caption='[[3dyb]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AD0:DIGALACTURONIC+ACID'>AD0</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyb OCA], [http://pdbe.org/3dyb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dyb RCSB], [http://www.ebi.ac.uk/pdbsum/3dyb PDBsum]</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=3dyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyb OCA], [http://pdbe.org/3dyb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dyb RCSB], [http://www.ebi.ac.uk/pdbsum/3dyb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dyb ProSAT]</span></td></tr>
 </table>
 == Function ==

3dyb

From Proteopedia

Revision as of 08:58, 25 October 2017

proteinase K- digalacturonic acid complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox