P56192: Methionine--tRNA ligase, cytoplasmic (MARS1)

Methionine--tRNA ligase, cytoplasmic (MARS1) is a 900-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P56192.

Gene
MARS1
Organism
Homo sapiens
Length
900 residues
Mean pLDDT
90.3
Model
AF-P56192-F1 v6
Model created
1 Aug 2025
PDB structures
7

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Model confidence (pLDDT)

The mean pLDDT of this model is 90.3 (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 accurate73%
70 to 90Confident: backbone generally right21%
50 to 70Low: treat with caution1%
Below 50Very low: often disordered regions4%

What pLDDT means and how to read it

Function

Catalyzes the specific attachment of L-methionine 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:11714285, PubMed:33909043). Plays a role in the synthesis of ribosomal RNA in the nucleolus (PubMed:10791971). In addition, can prevent the misincorporation of homocysteine into tRNA and protein by catalyzing a tRNA-independent hydrolysis of the misactivated homocysteinyl-AMP intermediate. The homocysteinyl-AMP intermediate undergoes an intramolecular cyclization reaction in which the thiolate side chain of homocysteine displaces the AMP group, forming homocysteine-thiolactone…

Subunit structure

Monomer (PubMed:11714285). Part of a multisubunit complex that groups tRNA ligases for Arg (RARS1), Asp (DARS1), Gln (QARS1), Ile (IARS1), Leu (LARS1), Lys (KARS1), Met (MARS1) the bifunctional ligase for Glu and Pro (EPRS1) and the auxiliary subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18 (PubMed:19131329, PubMed:19289464, PubMed:26472928, Ref.26). Forms a linear complex that contains MARS1,…

Subcellular location

Cytoplasm, cytosol, Nucleus, nucleolus

Disease associations

Experimental structures in the PDB

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

PDB IDMethodResolutionChains and residues
4BVXX-ray1.6 ÅA=1-207
4BL7X-ray1.89 ÅA=1-224
4BVYX-ray1.99 ÅA=1-225
5GL7X-ray2.01 ÅA=221-834
5GOYX-ray2.28 ÅA=221-834
5Y6LX-ray2.9 ÅA=1-224
2DJVNMRA=835-900

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