1fma: Difference between revisions

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[[Image:1fma.png|left|200px]]


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==MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)==
The line below this paragraph, containing "STRUCTURE_1fma", creates the "Structure Box" on the page.
<StructureSection load='1fma' size='340' side='right'caption='[[1fma]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1fma]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FMA FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
{{STRUCTURE_1fma|  PDB=1fma  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fma OCA], [https://pdbe.org/1fma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fma RCSB], [https://www.ebi.ac.uk/pdbsum/1fma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fma ProSAT]</span></td></tr>
 
</table>
===MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)===
== Function ==
 
[https://www.uniprot.org/uniprot/MOAD_ECOLI MOAD_ECOLI] Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.<ref>PMID:17223713</ref>
 
== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
The line below this paragraph, {{ABSTRACT_PUBMED_11135669}}, adds the Publication Abstract to the page
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fm/1fma_consurf.spt"</scriptWhenChecked>
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    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1FMA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMA OCA].  
</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=1fma ConSurf].
 
<div style="clear:both"></div>
==Reference==
== References ==
Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation., Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H, Nat Struct Biol. 2001 Jan;8(1):42-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11135669 11135669]
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Rajagolpalan, K V.]]
[[Category: Rajagolpalan KV]]
[[Category: Rudolph, M J.]]
[[Category: Rudolph MJ]]
[[Category: Schindelin, H.]]
[[Category: Schindelin H]]
[[Category: Wuebbens, M M.]]
[[Category: Wuebbens MM]]
[[Category: Isopeptide bond]]
[[Category: Molybdenum cofactor biosynthesis]]
[[Category: Transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:28:39 2008''

Latest revision as of 10:16, 7 February 2024

MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)

Structural highlights

1fma is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.58Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MOAD_ECOLI Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Schmitz J, Wuebbens MM, Rajagopalan KV, Leimkuhler S. Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold. Biochemistry. 2007 Jan 23;46(3):909-16. PMID:17223713 doi:http://dx.doi.org/10.1021/bi062011w

1fma, resolution 1.58Å

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