4nr1
From Proteopedia
(Difference between revisions)
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==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide== | ==Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide== | ||
- | <StructureSection load='4nr1' size='340' side='right' caption='[[4nr1]], [[Resolution|resolution]] 2.68Å' scene=''> | + | <StructureSection load='4nr1' size='340' side='right'caption='[[4nr1]], [[Resolution|resolution]] 2.68Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[4nr1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NR1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nr1]] is a 2 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=4NR1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NR1 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DYL:(2R)-2-AMINOPENT-4-ENOIC+ACID'>DYL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jaa|4jaa]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jaa|4jaa]]</td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FIH1, HIF1AN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hypoxia-inducible_factor-asparagine_dioxygenase Hypoxia-inducible factor-asparagine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.30 1.14.11.30] </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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [http://pdbe.org/4nr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 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=4nr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nr1 OCA], [http://pdbe.org/4nr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nr1 RCSB], [http://www.ebi.ac.uk/pdbsum/4nr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nr1 ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Human]] | ||
[[Category: Hypoxia-inducible factor-asparagine dioxygenase]] | [[Category: Hypoxia-inducible factor-asparagine dioxygenase]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: McDonough, M A]] | [[Category: McDonough, M A]] | ||
[[Category: Schofield, C J]] | [[Category: Schofield, C J]] |
Revision as of 08:45, 10 April 2019
Factor inhibiting HIF-1 alpha in complex with consensus ankyrin repeat domain-(d)allyl-GLY peptide
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Categories: Human | Hypoxia-inducible factor-asparagine dioxygenase | Large Structures | McDonough, M A | Schofield, C J | Scotti, J S | Activator-inhibitor | Ard | Asparaginyl/aspartyl hydroxylase | Beta-hydroxylation | Dioxygenase | Dna-binding | Dsbh | Epigenetic regulation | Facial triad | Helix-loop-helix-beta | Metal-binding | On-heme | Oxidoreductase | Oxidoreductase-peptide complex | Oxygenase | Signaling | Transcription