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:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-520003 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Eukaryotic translation elongation factor 1 epsilon-1
Molecule details ›
Chains: A, C, E, G
Length: 171 amino acids
Theoretical weight: 19.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Nuclear-export cofactor Arc1p
Structure domains:
Length: 171 amino acids
Theoretical weight: 19.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
O43324 (Residues: 1-169; Coverage: 97%)
Sequence domains: Nuclear-export cofactor Arc1p
Structure domains:
Bifunctional glutamate/proline--tRNA ligase
Molecule details ›
Chains: B, D, F, H
Length: 175 amino acids
Theoretical weight: 19.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Nuclear-export cofactor Arc1p
Structure domains: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Length: 175 amino acids
Theoretical weight: 19.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P07814 (Residues: 1-175; Coverage: 12%)
Sequence domains: Nuclear-export cofactor Arc1p
Structure domains: Glutathione S-transferase Yfyf (Class Pi); Chain A, domain 2
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PAL/PLS BEAMLINE 5C (4A)
Spacegroup:
P31
Expression system: Escherichia coli
