3rk8

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==Crystal structure of the chloride inhibited dihydrodipicolinate synthase from Acinetobacter baumannii complexed with pyruvate at 1.8 A resolution==
==Crystal structure of the chloride inhibited dihydrodipicolinate synthase from Acinetobacter baumannii complexed with pyruvate at 1.8 A resolution==
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<StructureSection load='3rk8' size='340' side='right' caption='[[3rk8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='3rk8' size='340' side='right'caption='[[3rk8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rk8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii_19606 Acinetobacter baumannii 19606]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3RK8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rk8]] 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=3RK8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RK8 FirstGlance]. <br>
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</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
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</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pud|3pud]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pud|3pud]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhdps, HMPREF0010_03414 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=575584 Acinetobacter baumannii 19606])</td></tr>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </span></td></tr>
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<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>
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<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=3rk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rk8 OCA], [http://pdbe.org/3rk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rk8 RCSB], [http://www.ebi.ac.uk/pdbsum/3rk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rk8 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rk8 OCA], [https://pdbe.org/3rk8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rk8 RCSB], [https://www.ebi.ac.uk/pdbsum/3rk8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rk8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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]
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[[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]]
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[[Category: Acinetobacter baumannii 19606]]
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[[Category: Acib2]]
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[[Category: Large Structures]]
[[Category: Kaur, P]]
[[Category: Kaur, P]]
[[Category: Kaushik, S]]
[[Category: Kaushik, S]]

Revision as of 10:14, 22 June 2022

Crystal structure of the chloride inhibited dihydrodipicolinate synthase from Acinetobacter baumannii complexed with pyruvate at 1.8 A resolution

PDB ID 3rk8

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