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.


2wa4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:49, 13 December 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='2wa4' size='340' side='right'caption='[[2wa4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='2wa4' size='340' side='right'caption='[[2wa4]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2wa4]] 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=2WA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WA4 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2wa4]] 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=2WA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WA4 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=069:N,3-DIHYDROXYBENZAMIDE'>069</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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]] 2.5&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mze|1mze]], [[2w0x|2w0x]], [[2cgn|2cgn]], [[1mzf|1mzf]], [[1h2n|1h2n]], [[1yci|1yci]], [[2wa3|2wa3]], [[2cgo|2cgo]], [[1h2k|1h2k]], [[1iz3|1iz3]], [[1h2m|1h2m]], [[1h2l|1h2l]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=069:N,3-DIHYDROXYBENZAMIDE'>069</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptide-aspartate_beta-dioxygenase Peptide-aspartate beta-dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.16 1.14.11.16] </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=2wa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wa4 OCA], [https://pdbe.org/2wa4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wa4 RCSB], [https://www.ebi.ac.uk/pdbsum/2wa4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wa4 ProSAT]</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=2wa4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wa4 OCA], [https://pdbe.org/2wa4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wa4 RCSB], [https://www.ebi.ac.uk/pdbsum/2wa4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wa4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN]] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref>
+
[https://www.uniprot.org/uniprot/HIF1N_HUMAN HIF1N_HUMAN] Hydroxylates HIF-1 alpha at 'Asp-803' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation. Positively regulates ASB4 activity, promoting vascular differentiation.<ref>PMID:12080085</ref> <ref>PMID:12042299</ref> <ref>PMID:17003112</ref> <ref>PMID:18299578</ref> <ref>PMID:19245366</ref> <ref>PMID:17573339</ref> <ref>PMID:21251231</ref> <ref>PMID:21177872</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 38: Line 37:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Peptide-aspartate beta-dioxygenase]]
+
[[Category: Clifton IJ]]
-
[[Category: Clifton, I J]]
+
[[Category: Conejo-Garcia A]]
-
[[Category: Conejo-Garcia, A]]
+
[[Category: Lienard BMR]]
-
[[Category: Lienard, B M.R]]
+
[[Category: McDonough MA]]
-
[[Category: McDonough, M A]]
+
[[Category: Schofield CJ]]
-
[[Category: Schofield, C J]]
+
-
[[Category: Dioxygenase]]
+
-
[[Category: Hydroxylase]]
+
-
[[Category: Hypoxia]]
+
-
[[Category: Oxidoreductase]]
+
-
[[Category: Transcription]]
+
-
[[Category: Transcription activator/inhibitor]]
+

Current revision

FACTOR INHIBITING HIF-1 ALPHA WITH N,3-dihydroxybenzamide

PDB ID 2wa4

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/2wa4"
Personal tools