5bmu

X-ray diffraction
2.6Å resolution

The crystal structure of the GST-like domains complex of AIMP3-EPRS mutant C92SC105SC123S

Released:
Model geometry
Fit model/data

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)

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-520003 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Eukaryotic translation elongation factor 1 epsilon-1 Chains: A, C, E, G
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:
  • Canonical: O43324 (Residues: 1-169; Coverage: 97%)
Gene names: AIMP3, EEF1E1, P18
Sequence domains: Nuclear-export cofactor Arc1p
Structure domains:
Bifunctional glutamate/proline--tRNA ligase Chains: B, D, F, H
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:
  • Canonical: P07814 (Residues: 1-175; Coverage: 12%)
Gene names: EPRS, EPRS1, GLNS, PARS, PIG32, QARS, QPRS
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

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P31
Unit cell:
a: 92.063Å b: 92.063Å c: 185.948Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.139 0.138 0.17
Expression system: Escherichia coli