6tp5 - Revision history

OCA at 13:06, 24 January 2024

OCA — Wed, 24 Jan 2024 13:06:30 GMT

←Older revision		Revision as of 13:06, 24 January 2024
Line 3:		Line 3:
	<StructureSection load='6tp5' size='340' side='right'caption='[[6tp5]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='6tp5' size='340' side='right'caption='[[6tp5]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6tp5]] is a 2 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=6TP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TP5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6tp5]] is a 2 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=6TP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TP5 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY~~</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU~~</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.25Å</td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">P4HTM~~, ~~PH4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~<~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>[https://en.wikipedia.org/wiki/Hypoxia-inducible_factor-proline_dioxygenase Hypoxia-inducible factor-proline dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.29 1.14.11.29] </~~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=6tp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp5 OCA], [https://pdbe.org/6tp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tp5 RCSB], [https://www.ebi.ac.uk/pdbsum/6tp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp5 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=6tp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp5 OCA], [https://pdbe.org/6tp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tp5 RCSB], [https://www.ebi.ac.uk/pdbsum/6tp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp5 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.	+	[https://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN] The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN]] Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.<ref>PMID:17726031</ref>	+	[https://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN] Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.<ref>PMID:17726031</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Hypoxia-inducible factor-proline dioxygenase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kallio~~, J P~~]]	+	[[Category: Kallio JP]]
-	[[Category: Koivunen, P]]	+	[[Category: Koivunen P]]
-	[[Category: Koski~~, M K~~]]	+	[[Category: Koski MK]]
-	[[Category: Myllyharju, J]]	+	[[Category: Myllyharju J]]
-	[[Category: Myllykoski, M]]	+	[[Category: Myllykoski M]]
-	[[Category: Raasakka, A]]	+	[[Category: Raasakka A]]
-	[[Category: Sutinen, A]]	+	[[Category: Sutinen A]]
-	[[Category: Wierenga~~, R K]]~~	+	[[Category: Wierenga RK]]
-	~~[[Category: 2-oxoglutarate-binding protein]]~~	+
-	~~[[Category: Calcium-binding protein]]~~	+
-	~~[[Category: Double-stranded beta helix]]~~	+
-	~~[[Category: Ef-hand]]~~	+
-	~~[[Category: Hidea syndrome]]~~	+
-	~~[[Category: Iron-binding protein]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Prolyl-4-hydroxylase]]~~	+
-	~~[[Category: Transmembrane protein~~]]	+

OCA at 09:05, 21 July 2021

OCA — Wed, 21 Jul 2021 09:05:47 GMT

←Older revision		Revision as of 09:05, 21 July 2021
Line 3:		Line 3:
	<StructureSection load='6tp5' size='340' side='right'caption='[[6tp5]], [[Resolution\|resolution]] 2.25Å' scene=''>		<StructureSection load='6tp5' size='340' side='right'caption='[[6tp5]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6tp5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TP5 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6TP5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6tp5]] is a 2 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=6TP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TP5 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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-proline_dioxygenase Hypoxia-inducible factor-proline dioxygenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.29 1.14.11.29] </span></td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">P4HTM, PH4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6tp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp5 OCA], [~~http~~://pdbe.org/6tp5 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6tp5 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6tp5 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp5 ProSAT]</span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hypoxia-inducible_factor-proline_dioxygenase Hypoxia-inducible factor-proline dioxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.29 1.14.11.29] </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=6tp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp5 OCA], [https://pdbe.org/6tp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tp5 RCSB], [https://www.ebi.ac.uk/pdbsum/6tp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp5 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.	+	[[https://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN]] Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.<ref>PMID:17726031</ref>	+	[[https://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN]] Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.<ref>PMID:17726031</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Hypoxia-inducible factor-proline dioxygenase]]		[[Category: Hypoxia-inducible factor-proline dioxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]

OCA at 06:56, 30 December 2020

OCA — Wed, 30 Dec 2020 06:56:52 GMT

←Older revision		Revision as of 06:56, 30 December 2020
Line 1:		Line 1:

	==Crystal structure of human Transmembrane prolyl 4-hydroxylase==		==Crystal structure of human Transmembrane prolyl 4-hydroxylase==
-	<StructureSection load='6tp5' size='340' side='right'caption='[[6tp5]]' scene=''>	+	<StructureSection load='6tp5' size='340' side='right'caption='[[6tp5]], [[Resolution\|resolution]] 2.25Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TP5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TP5 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6tp5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TP5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TP5 FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp5 OCA], [http://pdbe.org/6tp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tp5 RCSB], [http://www.ebi.ac.uk/pdbsum/6tp5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp5 ProSAT]</span></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=OGA:N-OXALYLGLYCINE'>OGA</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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-proline_dioxygenase Hypoxia-inducible factor-proline dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.29 1.14.11.29] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp5 OCA], [http://pdbe.org/6tp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tp5 RCSB], [http://www.ebi.ac.uk/pdbsum/6tp5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp5 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN]] The disease is caused by mutations affecting the gene represented in this entry.
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/P4HTM_HUMAN P4HTM_HUMAN]] Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.<ref>PMID:17726031</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Prolyl 4-hydroxylases (P4Hs) catalyze post-translational hydroxylation of peptidyl proline residues. In addition to collagen P4Hs and hypoxia-inducible factor P4Hs, a third P4H; the poorly characterized endoplasmic reticulum (ER)-localized transmembrane prolyl 4-hydroxylase (P4H-TM); is found in animals. P4H-TM variants are associated with the familiar neurological HIDEA syndrome, but how these variants might contribute to disease is unknown. Here, we explored this question in a structural and functional analysis of soluble human P4H-TM. The crystal structure revealed an EF-domain with two Ca2+-binding motifs inserted within the catalytic domain. A substrate-binding groove was formed between the EF-domain and the conserved core of the catalytic domain. The proximity of the EF-domain to the active site suggests that Ca2+-binding is relevant to the catalytic activity. Functional analysis demonstrated that Ca2+-binding affinity of P4H-TM is within the range of physiological Ca2+ concentration in the ER. P4H-TM was found both as a monomer and a dimer in solution, but the monomer-dimer equilibrium was not regulated by Ca2+. The catalytic site contained bound Fe2+ and N-oxalylglycine, which is an analogue of the cosubstrate 2-oxoglutarate. Comparison to homologous P4H structures complexed with peptide substrates showed that the substrate interacting residues and the lid structure that folds over the substrate are conserved in P4H-TM, whereas the extensive loop structures that surround the substrate-binding groove, generating a negative surface potential, are different. Analysis of the structure suggests that the HIDEA variants cause loss of P4H-TM function. In conclusion, P4H-TM shares key structural elements with other P4Hs while having an unique EF-domain.
		+
		+	Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains.,Myllykoski M, Sutinen A, Koski MK, Kallio JP, Raasakka A, Myllyharju J, Wierenga RK, Koivunen P J Biol Chem. 2020 Dec 17. pii: RA120.016542. doi: 10.1074/jbc.RA120.016542. PMID:33334883<ref>PMID:33334883</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6tp5" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Hypoxia-inducible factor-proline dioxygenase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Kallio JP]]	+	[[Category: Kallio, J P]]
-	[[Category: Koivunen P]]	+	[[Category: Koivunen, P]]
-	[[Category: Koski MK]]	+	[[Category: Koski, M K]]
-	[[Category: Myllyharju J]]	+	[[Category: Myllyharju, J]]
-	[[Category: Myllykoski M]]	+	[[Category: Myllykoski, M]]
-	[[Category: Raasakka A]]	+	[[Category: Raasakka, A]]
-	[[Category: Sutinen A]]	+	[[Category: Sutinen, A]]
-	[[Category: Wierenga RK]]	+	[[Category: Wierenga, R K]]
		+	[[Category: 2-oxoglutarate-binding protein]]
		+	[[Category: Calcium-binding protein]]
		+	[[Category: Double-stranded beta helix]]
		+	[[Category: Ef-hand]]
		+	[[Category: Hidea syndrome]]
		+	[[Category: Iron-binding protein]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Prolyl-4-hydroxylase]]
		+	[[Category: Transmembrane protein]]

OCA at 10:28, 24 December 2020

OCA — Thu, 24 Dec 2020 10:28:13 GMT

←Older revision		Revision as of 10:28, 24 December 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6tp5 is ~~ON HOLD until Paper Publication~~	+	==Crystal structure of human Transmembrane prolyl 4-hydroxylase==
-		+	<StructureSection load='6tp5' size='340' side='right'caption='[[6tp5]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TP5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6TP5 FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6tp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tp5 OCA], [http://pdbe.org/6tp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tp5 RCSB], [http://www.ebi.ac.uk/pdbsum/6tp5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tp5 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Kallio JP]]
		+	[[Category: Koivunen P]]
		+	[[Category: Koski MK]]
		+	[[Category: Myllyharju J]]
		+	[[Category: Myllykoski M]]
		+	[[Category: Raasakka A]]
		+	[[Category: Sutinen A]]
		+	[[Category: Wierenga RK]]

OCA at 06:19, 22 July 2020

OCA — Wed, 22 Jul 2020 06:19:48 GMT

←Older revision		Revision as of 06:19, 22 July 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6tp5 is ON HOLD	+	The entry 6tp5 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6tp5" [edit=sysop:move=sysop]

OCA — Wed, 18 Dec 2019 05:57:38 GMT

Protected "6tp5" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:57, 18 December 2019

OCA: New page: '''Unreleased structure''' The entry 6tp5 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 18 Dec 2019 05:57:36 GMT

New page: '''Unreleased structure''' The entry 6tp5 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6tp5 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]