View source for 5ssx


==Crystal Structure human formylglycine generating enzyme E130D mutant==
<StructureSection load='5ssx' size='340' side='right'caption='[[5ssx]], [[Resolution|resolution]] 1.02&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ssx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SSX 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]] 1.02&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=5ssx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ssx OCA], [https://pdbe.org/5ssx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ssx RCSB], [https://www.ebi.ac.uk/pdbsum/5ssx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ssx ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN] Defects in SUMF1 are the cause of multiple sulfatase deficiency (MSD) [MIM:[https://omim.org/entry/272200 272200]. MSD is a clinically and biochemically heterogeneous disorder caused by the simultaneous impairment of all sulfatases, due to defective post-translational modification and activation. It combines features of individual sulfatase deficiencies such as metachromatic leukodystrophy, mucopolysaccharidosis, chondrodysplasia punctata, hydrocephalus, ichthyosis, neurologic deterioration and developmental delay. Inheritance is autosomal recessive.<ref>PMID:12757706</ref> <ref>PMID:12757705</ref> <ref>PMID:15146462</ref> <ref>PMID:18157819</ref> 
== Function ==
[https://www.uniprot.org/uniprot/SUMF1_HUMAN SUMF1_HUMAN] Using molecular oxygen and an unidentified reducing agent, oxidizes a cysteine residue in the substrate sulfatase to an active site 3-oxoalanine residue, which is also called C(alpha)-formylglycine. Known substrates include GALNS, ARSA, STS and ARSE.<ref>PMID:12757706</ref> <ref>PMID:15657036</ref> 

==See Also==
*[[Sulfatase-modifying factor|Sulfatase-modifying factor]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Radhakrishnan K]]
[[Category: Rudolph MG]]
[[Category: Schlotawa L]]