2g4o

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:26, 14 February 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='2g4o' size='340' side='right'caption='[[2g4o]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2g4o' size='340' side='right'caption='[[2g4o]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2g4o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G4O FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2g4o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G4O FirstGlance]. <br>
-
</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=SO4:SULFATE+ION'>SO4</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&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2g4h|2g4h]], [[2g4i|2g4i]], [[2g4j|2g4j]], [[2g4k|2g4k]], [[2g4l|2g4l]], [[2g4m|2g4m]], [[2g4n|2g4n]], [[2g4p|2g4p]], [[2g4q|2g4q]], [[2g4r|2g4r]], [[2g4s|2g4s]], [[2g4t|2g4t]], [[2g4u|2g4u]], [[2g4v|2g4v]], [[2g4w|2g4w]], [[2g4x|2g4x]], [[2g4y|2g4y]], [[2g4z|2g4z]], [[2g51|2g51]], [[2g52|2g52]], [[2g55|2g55]]</div></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=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">leuB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] </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=2g4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g4o OCA], [https://pdbe.org/2g4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g4o RCSB], [https://www.ebi.ac.uk/pdbsum/2g4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g4o 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=2g4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g4o OCA], [https://pdbe.org/2g4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g4o RCSB], [https://www.ebi.ac.uk/pdbsum/2g4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g4o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/LEU3_MYCTU LEU3_MYCTU]] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01035]
+
[https://www.uniprot.org/uniprot/LEU3_MYCTU LEU3_MYCTU] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01035]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 22: Line 20:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2g4o ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2g4o ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
-
<div style="background-color:#fffaf0;">
 
-
== Publication Abstract from PubMed ==
 
-
23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.
 
- 
-
On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.,Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674<ref>PMID:17327674</ref>
 
- 
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
-
</div>
 
-
<div class="pdbe-citations 2g4o" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Isopropylmalate dehydrogenase|Isopropylmalate dehydrogenase]]
*[[Isopropylmalate dehydrogenase|Isopropylmalate dehydrogenase]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: 3-isopropylmalate dehydrogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Mueller-Dieckmann, C]]
+
[[Category: Mycobacterium tuberculosis]]
-
[[Category: Weiss, M S]]
+
[[Category: Mueller-Dieckmann C]]
-
[[Category: Anomalous substructure of 3-isopropylmalate dehydrogenase]]
+
[[Category: Weiss MS]]
-
[[Category: Oxidoreductase]]
+

Current revision

anomalous substructure of 3-ISOPROPYLMALATE DEHYDROGENASE

PDB ID 2g4o

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools