Function and Biology Details
Reactions catalysed:
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Biochemical function:
- not assigned
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139772 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Bifunctional glutamate/proline--tRNA ligase
Molecule details ›
Chains: A, C, E, G
Length: 175 amino acids
Theoretical weight: 19.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Length: 175 amino acids
Theoretical weight: 19.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P07814 (Residues: 1-175; Coverage: 12%)
Structure domains: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
Molecule details ›
Chains: B, D, F, H
Length: 240 amino acids
Theoretical weight: 26.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Length: 240 amino acids
Theoretical weight: 26.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q13155 (Residues: 90-320; Coverage: 72%)
Sequence domains:
Structure domains: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
