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1i9c

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GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i9c"

Categories: Clostridium cochlearium | Large Structures | Gruber K | Kratky C

@@ Line 3: / Line 3: @@
 <StructureSection load='1i9c' size='340' side='right'caption='[[1i9c]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1i9c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cochlearius"_douglas_et_al._in_bulloch_et_al._1919 "bacillus cochlearius" douglas et al. in bulloch et al. 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I9C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1i9c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_cochlearium Clostridium cochlearium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I9C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I9C FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2AS:(2S,3S)-3-METHYL-ASPARTIC+ACID'>2AS</scene>, <scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</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]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ccw|1ccw]], [[1cb7|1cb7]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2AS:(2S,3S)-3-METHYL-ASPARTIC+ACID'>2AS</scene>, <scene name='pdbligand=5AD:5-DEOXYADENOSINE'>5AD</scene>, <scene name='pdbligand=B12:COBALAMIN'>B12</scene>, <scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLMS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1494 "Bacillus cochlearius" Douglas et al. in Bulloch et al. 1919]), GLME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1494 "Bacillus cochlearius" Douglas et al. in Bulloch et al. 1919])</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=1i9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9c OCA], [https://pdbe.org/1i9c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i9c RCSB], [https://www.ebi.ac.uk/pdbsum/1i9c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9c 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/Methylaspartate_mutase Methylaspartate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.1 5.4.99.1] </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=1i9c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i9c OCA], [http://pdbe.org/1i9c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i9c RCSB], [http://www.ebi.ac.uk/pdbsum/1i9c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i9c ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GMSS_CLOCO GMSS_CLOCO]] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526]<ref>PMID:1315276</ref> <ref>PMID:7880251</ref> <ref>PMID:8013871</ref>  [[http://www.uniprot.org/uniprot/GLME_CLOCO GLME_CLOCO]] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).<ref>PMID:7880251</ref> <ref>PMID:1315276</ref>
+[https://www.uniprot.org/uniprot/GMSS_CLOCO GMSS_CLOCO] Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).[HAMAP-Rule:MF_00526]<ref>PMID:1315276</ref> <ref>PMID:7880251</ref> <ref>PMID:8013871</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 26: / Line 24: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus cochlearius douglas et al. in bulloch et al. 1919]]
+[[Category: Clostridium cochlearium]]
 [[Category: Large Structures]]
-[[Category: Methylaspartate mutase]]
+[[Category: Gruber K]]
-[[Category: Gruber, K]]
+[[Category: Kratky C]]
-[[Category: Kratky, C]]
-[[Category: Coenzyme b12]]
-[[Category: Isomerase]]
-[[Category: Radical reaction]]
-[[Category: Ribose pseudorotation]]
-[[Category: Rossman-fold]]
-[[Category: Tim-barrel]]

1i9c

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GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM: COMPLEX WITH ADENOSYLCOBALAMIN AND SUBSTRATE

Structural highlights

Function

Evolutionary Conservation

References

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