4g38
From Proteopedia
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| - | [[Image:4g38.jpg|left|200px]] | ||
| - | + | ==Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer== | |
| - | + | <StructureSection load='4g38' size='340' side='right'caption='[[4g38]], [[Resolution|resolution]] 1.56Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4g38]] 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=4G38 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G38 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.56Å</td></tr> | |
| - | + | <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> | |
| - | == | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4g38 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g38 OCA], [https://pdbe.org/4g38 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g38 RCSB], [https://www.ebi.ac.uk/pdbsum/4g38 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g38 ProSAT]</span></td></tr> |
| - | [[4g38]] is a 1 chain structure with sequence from [ | + | </table> |
| - | [[ | + | == Function == |
| - | [[ | + | [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] |
| - | [[ | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| + | [[Category: Smith KW]] | ||
| + | [[Category: Stroupe ME]] | ||
Current revision
Mutational analysis of sulfite reductase hemoprotein reveals the mechanism for coordinated electron and proton transfer
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