4qgn

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==Human acireductone dioxygenase with iron ion and L-methionine in active center==
==Human acireductone dioxygenase with iron ion and L-methionine in active center==
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<StructureSection load='4qgn' size='340' side='right' caption='[[4qgn]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
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<StructureSection load='4qgn' size='340' side='right'caption='[[4qgn]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qgn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
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<table><tr><td colspan='2'>[[4qgn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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>
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</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>
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</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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADI1, HMFT1638, MTCBP1, NP_060739 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADI1, HMFT1638, MTCBP1, NP_060739 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<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>
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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/Acireductone_dioxygenase_(Fe(2+)-requiring) Acireductone dioxygenase (Fe(2+)-requiring)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.54 1.13.11.54] </span></td></tr>
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<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://pdbe.org/4qgn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qgn RCSB], [http://www.ebi.ac.uk/pdbsum/4qgn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qgn ProSAT]</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=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 ==
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[[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>
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[[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>
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==See Also==
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Borowski, T]]
[[Category: Borowski, T]]
[[Category: Chruszcz, M]]
[[Category: Chruszcz, M]]

Revision as of 10:05, 13 April 2022

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

PDB ID 4qgn

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