3n58

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:08, 6 September 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Crystal structure of S-ADENOSYL-L-HOMOCYSTEINE hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form==
==Crystal structure of S-ADENOSYL-L-HOMOCYSTEINE hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form==
-
<StructureSection load='3n58' size='340' side='right' caption='[[3n58]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
+
<StructureSection load='3n58' size='340' side='right'caption='[[3n58]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3n58]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Brua2 Brua2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N58 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N58 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3n58]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_2308 Brucella abortus 2308]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N58 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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]] 2.39&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ahcY, BAB1_2099 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=359391 BRUA2])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </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=3n58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n58 OCA], [https://pdbe.org/3n58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n58 RCSB], [https://www.ebi.ac.uk/pdbsum/3n58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n58 ProSAT]</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=3n58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n58 OCA], [http://pdbe.org/3n58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n58 RCSB], [http://www.ebi.ac.uk/pdbsum/3n58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n58 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/SAHH_BRUA2 SAHH_BRUA2]] May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine (By similarity).
+
[https://www.uniprot.org/uniprot/SAHH_BRUA2 SAHH_BRUA2] May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
-
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/3n58_consurf.spt"</scriptWhenChecked>
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/3n58_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
Line 26: Line 25:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Adenosylhomocysteinase]]
+
[[Category: Brucella abortus 2308]]
-
[[Category: Brua2]]
+
[[Category: Large Structures]]
-
[[Category: Structural genomic]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Ssgcid]]
+

Current revision

Crystal structure of S-ADENOSYL-L-HOMOCYSTEINE hydrolase from brucella melitensis in ternary complex with NAD and adenosine, orthorhombic form

PDB ID 3n58

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools