4g39

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m (Protected "4g39" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 4g39 is ON HOLD
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==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer==
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<StructureSection load='4g39' size='340' side='right'caption='[[4g39]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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Authors: Smith, K.W., Stroupe, M.E.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4g39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G39 FirstGlance]. <br>
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Description: Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SRM:SIROHEME'>SRM</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g39 OCA], [https://pdbe.org/4g39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g39 RCSB], [https://www.ebi.ac.uk/pdbsum/4g39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g39 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYSI_ECOLI CYSI_ECOLI] Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate.[HAMAP-Rule:MF_01540]
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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[[Category: Smith KW]]
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[[Category: Stroupe ME]]

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Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer

PDB ID 4g39

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