LH3 ASP392ALA
SiMPLOD ID   This is the unique identifier for this mutation in the SiMPLOD database. Please use this identifier when linking information described in SiMPLOD about this mutation.	SiMPLOD3-277
Isoenzyme   Follow the links to gather information about the LH3 isoenzyme	Lysyl Hydroxylase 3 (human) - UniProt - Full Info
Mutation type   Current information about the clinical implications of the mutation	Mutation for Biochemical Studies (not necessarily related to observed polymorphisms)
Evidence at protein level   Based on available structural and biochemical information, a statement about the existence of an LH enzyme variant bearing the described mutation is provided	This variant EXISTS at the protein level: published experimental data support its existence as protein product.
LH Activity   When available, biochemical data describing the lysyl hydroxylase activity of the mutant are reported	No experimental data available
GT/GGT Activity   When available, biochemical data describing the galactosyltransferase (GT) and glucosylgalactosyltransferase (GGT) activities of the mutant are reported	++
References   Publications (and associated links) describing the mutation	Wang et al., 2002 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	Wang et al. adopted site-directed mutagenesis approach to identify key residue in PLOD activity. Mutation of Asp392 indicate that the DXD-like motif at position 392–394 is not important for glycosyltranferase activity. Indeed these residues map in the accessory domain.
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-73: LH1 ASP382ALA (Uncertain significance) SiMPLOD1-74: LH1 ASP382GLY (Uncertain significance) SiMPLOD1-134: LH1 dupl326-585;TYR455THRFS (Pathogenic) SiMPLOD1-320: LH1 delta367-443 (Pathogenic) SiMPLOD3-597: LH3 ASP392ASP (SNP)
Last Update   An evaluation of the possible effects/implications of the mutations on the LH3 molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH3 (generated using the crystal structure of full-length human LH3 as template). You may select a different PDB model file to visualize the mutation(s) using the drop-down menu below (page will refresh): LH3 homology modelLH3 with Fe2+ and 2-OG (PDB 6FXK)LH3 with Fe2+, 2-OG and Mn2+ (PDB 6FXM)LH3 with Fe2+, 2-OG, Mn2+ and UDP-Gal (PDB 6FXR)LH3 with Fe2+, 2-OG, Mn2+ and UDP-Glc (PDB 6FXT)