SiMPLOD v. 0.6.2 alpha

LH1 TRP521END

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.
SiMPLOD1-204

Isoenzyme
  Follow the links to gather information about the LH1 isoenzyme
Lysyl Hydroxylase 1 (human) - UniProt - Full Info

Nucleotide mutation
  Follow the links to explore annotated information about the significance of the PLOD1 c.1562G>A mutation
PLOD1 NM_000302.2:c.1562G>A - NCBI RefSeq
NCBI SNP: rs1057518879
NCBI ClinVar: 374077

Mutation type
  Current information about the clinical implications of the mutation
Pathogenic

LOVD
  Link to Leiden Open Variation Database (LOVD)
c.1563G>A

Disease Phenotype
  Annotated information about disease phenotypes associated to this mutation
Neonatal hypotonia Link1 Link2

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
Warning: this variant incorporates a premature truncation of the aminoacid sequence at residue 521, and may result in misfolding and/or complete absence of the enzyme.

This variant is EXTREMELY UNLIKELY to be compatible with a folded LH enzyme. The representation shown in the structure viewer is therefore for mere display purposes and does not refer to an actual predicted existing protein product.

Structural Observations
  An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure

Related Entries
  A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized
SiMPLOD1-134: LH1 dupl326-585;TYR455THRFS (Pathogenic)
SiMPLOD1-325: LH1 delta491-550 (Pathogenic)

Last Update
  An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure
2021-06-23 08:38:51

The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH1 (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):

LH1 TRP521END
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.	SiMPLOD1-204
Isoenzyme Follow the links to gather information about the LH1 isoenzyme	Lysyl Hydroxylase 1 (human) - UniProt - Full Info
Nucleotide mutation Follow the links to explore annotated information about the significance of the PLOD1 c.1562G>A mutation	PLOD1 NM_000302.2:c.1562G>A - NCBI RefSeq NCBI SNP: rs1057518879 NCBI ClinVar: 374077
Mutation type Current information about the clinical implications of the mutation	Pathogenic
LOVD Link to Leiden Open Variation Database (LOVD)	c.1563G>A
Disease Phenotype Annotated information about disease phenotypes associated to this mutation	Neonatal hypotonia Link1 Link2
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	Warning: this variant incorporates a premature truncation of the aminoacid sequence at residue 521, and may result in misfolding and/or complete absence of the enzyme. This variant is EXTREMELY UNLIKELY to be compatible with a folded LH enzyme. The representation shown in the structure viewer is therefore for mere display purposes and does not refer to an actual predicted existing protein product.
Structural Observations An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure
Related Entries A list of related LH/PLOD variants found matching the structural position of the mutation currently visualized	SiMPLOD1-134: LH1 dupl326-585;TYR455THRFS (Pathogenic) SiMPLOD1-325: LH1 delta491-550 (Pathogenic)
Last Update An evaluation of the possible effects/implications of the mutations on the LH1 molecular structure	2021-06-23 08:38:51
The three-dimensional visualization is currently based on the homology model of full-length, dimeric human LH1 (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):