LH3 ASP190ALA
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.	SiMPLOD3-270
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 aspartates at position 187-191 eliminated the glycosyltrasferase activity. Despite not being involved in Mn2+ coordination these residues are close to the glycosyltransferase active site.
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-178: LH1 SER178ARG (Uncertain significance) SiMPLOD1-179: LH1 SER178ARG (SNP) SiMPLOD1-180: LH1 SER178SER (Likely benign) SiMPLOD2-1082: LH2a ASP190VAL (SNP) SiMPLOD3-309: LH3 ASP190ASP (benign) SiMPLOD3-310: LH3 ASP190GLU (SNP) SiMPLOD3-593: LH3 ASP190ASN (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)