Q15046: Lysine--tRNA ligase (KARS1)

Lysine--tRNA ligase (KARS1) is a 597-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q15046.

Gene
KARS1
Organism
Homo sapiens
Length
597 residues
Mean pLDDT
90.5
Model
AF-Q15046-F1 v6
Model created
1 Aug 2025
PDB structures
14

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.5 (very high overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate82%
70 to 90Confident: backbone generally right8%
50 to 70Low: treat with caution2%
Below 50Very low: often disordered regions8%

What pLDDT means and how to read it

Function

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA (PubMed:18029264, PubMed:18272479, PubMed:9278442). When secreted, acts as a signaling molecule that induces immune response through the activation of monocyte/macrophages (PubMed:15851690). Catalyzes the synthesis of the signaling molecule diadenosine tetraphosphate (Ap4A), and thereby mediates disruption of the complex between HINT1 and MITF and the concomitant activation of MITF transcriptional activity (PubMed:14975237, PubMed:19524539, PubMed:23159739, PubMed:5338216)

Subunit structure

Homodimer and tetradimer (PubMed:18272479, PubMed:23159739, PubMed:26074468, PubMed:28887846). Part of the multisynthetase complex (MSC), a multisubunit complex that groups tRNA ligases for Arg (RARS), Asp (DARS), Gln (QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the bifunctional ligase for Glu and Pro (EPRS) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18…

Subcellular location

Cytoplasm, cytosol, Cytoplasm, Nucleus, Cell membrane, Secreted, Mitochondrion

Disease associations

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6ILDX-ray1.88 ÅA/B=70-581
4YCUX-ray2.1 ÅA/B=70-581
8XP4X-ray2.26 ÅA/B=70-580
3BJUX-ray2.31 ÅA/B/C/D=70-582
6CHDX-ray2.5 ÅA/B=1-597
6ILHX-ray2.5 ÅA/B=70-581
7EA9X-ray2.5 ÅA/B/C/D=70-581
8HYRX-ray2.55 ÅA/B=70-580
9DPLEM2.8 ÅA/B=1-597
4DPGX-ray2.84 ÅA/B/C/D/E/F/G/H=70-581
4YCWX-ray2.9 ÅA/B/E/F=70-581
9DPBEM2.9 ÅA/B=1-597
9DPAEM3.0 ÅA/B=1-597
9DOWEM3.1 ÅA/B=1-597

More AlphaFold highlights

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