5ktp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:54, 27 September 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5ktp' size='340' side='right'caption='[[5ktp]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
<StructureSection load='5ktp' size='340' side='right'caption='[[5ktp]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5ktp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KTP FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5ktp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KTP FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ITN:2-METHYLIDENEBUTANEDIOIC+ACID'>ITN</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 1.542&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kts|5kts]], [[5ktm|5ktm]], [[5ktt|5ktt]], [[5ktr|5ktr]], [[5kto|5kto]], [[5ktn|5ktn]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ITN:2-METHYLIDENEBUTANEDIOIC+ACID'>ITN</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nadA, PH0013 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=70601 Pyrococcus horikoshii])</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=5ktp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ktp OCA], [https://pdbe.org/5ktp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ktp RCSB], [https://www.ebi.ac.uk/pdbsum/5ktp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ktp ProSAT]</span></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Quinolinate_synthase Quinolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.72 2.5.1.72] </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=5ktp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ktp OCA], [http://pdbe.org/5ktp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ktp RCSB], [http://www.ebi.ac.uk/pdbsum/5ktp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ktp ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/NADA_PYRHO NADA_PYRHO]] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity).
+
[https://www.uniprot.org/uniprot/NADA_PYRHO NADA_PYRHO] Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 26: Line 24:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Pyrococcus horikoshii]]
+
[[Category: Pyrococcus horikoshii OT3]]
-
[[Category: Quinolinate synthase]]
+
[[Category: Ealick SE]]
-
[[Category: Ealick, S E]]
+
[[Category: Fenwick MK]]
-
[[Category: Fenwick, M K]]
+
-
[[Category: Biosynthetic enzyme]]
+
-
[[Category: Dehydratase]]
+
-
[[Category: Iron-sulfur cluster]]
+
-
[[Category: Substrate analog complex]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of Pyrococcus horikoshii quinolinate synthase (NadA) with bound itaconate and Fe4S4 cluster

PDB ID 5ktp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools