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.


4qgn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:50, 9 August 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Human acireductone dioxygenase with iron ion and L-methionine in active center==
==Human acireductone dioxygenase with iron ion and L-methionine in active center==
-
<StructureSection load='4qgn' size='340' side='right' caption='[[4qgn]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
+
<StructureSection load='4qgn' size='340' side='right'caption='[[4qgn]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4qgn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QGN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QGN FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4qgn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QGN FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 3.05&#8491;</td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acireductone_dioxygenase_(Fe(2+)-requiring) Acireductone dioxygenase (Fe(2+)-requiring)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.54 1.13.11.54] </span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4qgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qgn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qgn RCSB], [http://www.ebi.ac.uk/pdbsum/4qgn PDBsum]</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=4qgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qgn OCA], [https://pdbe.org/4qgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qgn RCSB], [https://www.ebi.ac.uk/pdbsum/4qgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qgn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/MTND_HUMAN MTND_HUMAN]] Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Also down-regulates cell migration mediated by MMP14. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line.[HAMAP-Rule:MF_03154]<ref>PMID:11602742</ref> <ref>PMID:15938715</ref>
+
[https://www.uniprot.org/uniprot/MTND_HUMAN MTND_HUMAN] Catalyzes the formation of formate and 2-keto-4-methylthiobutyrate (KMTB) from 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene). Also down-regulates cell migration mediated by MMP14. Necessary for hepatitis C virus replication in an otherwise non-permissive cell line.[HAMAP-Rule:MF_03154]<ref>PMID:11602742</ref> <ref>PMID:15938715</ref>
 +
 
 +
==See Also==
 +
*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Borowski, T]]
+
[[Category: Homo sapiens]]
-
[[Category: Chruszcz, M]]
+
[[Category: Large Structures]]
-
[[Category: Milaczewska, A M]]
+
[[Category: Borowski T]]
-
[[Category: Minor, W]]
+
[[Category: Chruszcz M]]
-
[[Category: Niedzialkowska, E]]
+
[[Category: Milaczewska AM]]
-
[[Category: Petkowski, J J]]
+
[[Category: Minor W]]
-
[[Category: Iron binding]]
+
[[Category: Niedzialkowska E]]
-
[[Category: Oxidoreductase]]
+
[[Category: Petkowski JJ]]
-
[[Category: Rmlc-like cupin]]
+

Current revision

Human acireductone dioxygenase with iron ion and L-methionine in active center

PDB ID 4qgn

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/4qgn"
Personal tools