LH2a ASP668ALA (LH2a) - ASP689ALA (LH2b)
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.	SiMPLOD2-336
Isoenzyme   Follow the links to gather information about the LH2a isoenzyme	Lysyl Hydroxylase 2a (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
References   Publications (and associated links) describing the mutation	Guo et al., 2018 - DOI - PubMed
Notes from publications   A curated excerpt with information about the mutation from the publications found above	To determine key residues in activity and dimerization Guo et al. performed site-directed mutagenesis on L230, a viral homolog of PLODs, and on PLOD2. The Asp689Ala (PLOD2b numbering) mutation disrupted the dimeric interface. This residue is involved in the coordination of the catalytic iron.
Structural Observations   An evaluation of the possible effects/implications of the mutations on the LH2a molecular structure	This residue involved in Fe2+ coordination in the LH domain.
Related Entries   A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-82: LH1 ASP658ALA (for biochemistry) SiMPLOD3-282: LH3 ASP669ALA (for biochemistry) SiMPLOD3-379: LH3 ASP669ASN (SNP) SiMPLOD3-380: LH3 ASP669HIS (SNP)
Last Update   An evaluation of the possible effects/implications of the mutations on the LH2a molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH2a (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): LH2a homology modelLH2b homology modelLH3 with Fe2+ and 2-OG (PDB 6FXK)