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==Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis str. Ames Ancestor==
==Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis str. Ames Ancestor==
<StructureSection load='4iqe' size='340' side='right' caption='[[4iqe]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='4iqe' size='340' side='right'caption='[[4iqe]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4iqe]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3kz2 3kz2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IQE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IQE FirstGlance]. <br>
<table><tr><td colspan='2'>[[4iqe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3kz2 3kz2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IQE FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.501&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4iqd|4iqd]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">prpB, yqiQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 "Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</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=4iqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iqe OCA], [https://pdbe.org/4iqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4iqe RCSB], [https://www.ebi.ac.uk/pdbsum/4iqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4iqe 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/Methylisocitrate_lyase Methylisocitrate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.30 4.1.3.30] </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=4iqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4iqe OCA], [http://pdbe.org/4iqe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4iqe RCSB], [http://www.ebi.ac.uk/pdbsum/4iqe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4iqe ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q81QR8_BACAN Q81QR8_BACAN]] Catalyzes the formation of pyruvate and succinate from 2-methylisocitrate.[RuleBase:RU361121]  
[https://www.uniprot.org/uniprot/A0A6L7HJ56_BACAN A0A6L7HJ56_BACAN] Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate.[RuleBase:RU361121]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Methylisocitrate lyase]]
[[Category: Bacillus anthracis]]
[[Category: Anderson, W F]]
[[Category: Large Structures]]
[[Category: Structural genomic]]
[[Category: Anderson WF]]
[[Category: Csgid]]
[[Category: CSGID]]
[[Category: Joachimiak, A]]
[[Category: Joachimiak A]]
[[Category: Kim, Y]]
[[Category: Kim Y]]
[[Category: Kwon, K]]
[[Category: Kwon K]]
[[Category: Maltseva, N]]
[[Category: Maltseva N]]
[[Category: Lyase]]
[[Category: National institute of allergy and infectious disease]]
[[Category: Niaid]]
[[Category: Tim barrel]]

Latest revision as of 18:28, 20 September 2023

Crystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis str. Ames AncestorCrystal Structure of Carboxyvinyl-Carboxyphosphonate Phosphorylmutase from Bacillus anthracis str. Ames Ancestor

Structural highlights

4iqe is a 2 chain structure with sequence from Bacillus anthracis. This structure supersedes the now removed PDB entry 3kz2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.501Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A6L7HJ56_BACAN Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate.[RuleBase:RU361121]

4iqe, resolution 2.50Å

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