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3tce
From Proteopedia
(Difference between revisions)
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==Crystal structure of the complex of Dihydrodipicolinate synthase from Acinetobacter baumannii with 5-Hydroxylysine at 2.6 A resolution== | ==Crystal structure of the complex of Dihydrodipicolinate synthase from Acinetobacter baumannii with 5-Hydroxylysine at 2.6 A resolution== | ||
| - | <StructureSection load='3tce' size='340' side='right' caption='[[3tce]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3tce' size='340' side='right'caption='[[3tce]], [[Resolution|resolution]] 2.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3tce]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3tce]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acib2 Acib2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TCE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYZ:5-HYDROXYLYSINE'>LYZ</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYZ:5-HYDROXYLYSINE'>LYZ</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rk8|3rk8]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rk8|3rk8]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhdps, HMPREF0010_03414 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhdps, HMPREF0010_03414 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=575584 ACIB2])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tce OCA], [https://pdbe.org/3tce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tce RCSB], [https://www.ebi.ac.uk/pdbsum/3tce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tce ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/D0CFC3_ACIBA D0CFC3_ACIBA]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA) (By similarity).[SAAS:SAAS020625_004_011311][HAMAP-Rule:MF_00418] |
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | [[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | ||
| - | [[Category: | + | [[Category: Acib2]] |
| + | [[Category: Large Structures]] | ||
[[Category: Kaur, P]] | [[Category: Kaur, P]] | ||
[[Category: Kaushik, S]] | [[Category: Kaushik, S]] | ||
Revision as of 16:51, 6 July 2022
Crystal structure of the complex of Dihydrodipicolinate synthase from Acinetobacter baumannii with 5-Hydroxylysine at 2.6 A resolution
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