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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P12063 New Search
3PDB entries
6Biological assembly
34chain/assembly records
UNP PDB Protein and construct Assembly Composition class Protein state Molecular copy count PDB declaration Consistency status
P12063 1y42 Tyrosyl-tRNA synthetase, mitochondrial Author chain X Reference sequence 33–423 1 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count
P12063 2rkj Tyrosyl-tRNA synthetase Author chain A Reference sequence 33–423 1 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain B Reference sequence 33–423 1 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain E Reference sequence 33–423 1 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain F Reference sequence 33–423 1 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain I Reference sequence 33–423 1 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain J Reference sequence 33–423 1 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain M Reference sequence 33–423 1 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain N Reference sequence 33–423 1 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain A Reference sequence 33–423 2 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain B Reference sequence 33–423 2 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain E Reference sequence 33–423 2 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain F Reference sequence 33–423 2 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain I Reference sequence 33–423 2 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain J Reference sequence 33–423 2 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain M Reference sequence 33–423 2 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain N Reference sequence 33–423 2 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain A Reference sequence 33–423 3 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain B Reference sequence 33–423 3 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain E Reference sequence 33–423 3 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain F Reference sequence 33–423 3 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain I Reference sequence 33–423 3 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain J Reference sequence 33–423 3 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain M Reference sequence 33–423 3 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain N Reference sequence 33–423 3 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain A Reference sequence 33–423 4 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain B Reference sequence 33–423 4 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain E Reference sequence 33–423 4 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain F Reference sequence 33–423 4 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain I Reference sequence 33–423 4 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain J Reference sequence 33–423 4 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain M Reference sequence 33–423 4 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 2rkj Tyrosyl-tRNA synthetase Author chain N Reference sequence 33–423 4 Protein–RNA Homooligomer Protein 2 RNA 2 tetrameric （4） Consistent with all polymers
P12063 4ojm Tyrosine--tRNA ligase, mitochondrial Author chain X Reference sequence 33–423 1 Protein homooligomer Homooligomer Protein 2 dimeric （2） Consistent with protein count

“Homomeric versus heteromeric classification follows protein identity; different constructs of the same UniProt entry still require comparison of reference-sequence ranges, mutations and missing segments. Assemblies marked for review remain visible but are not included in the highest-confidence candidate set.