› 5t5s

X-ray diffraction
2.2Å resolution

A fragment of a human tRNA synthetase

Released:
DOI: 10.2210/pdb5t5s/pdb
PDB entry 5t5s coloured by chain, front view.
PDB entry 5t5s coloured by chain, side view.
PDB entry 5t5s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS.
Sun L, Song Y, Blocquel D, Yang XL, Schimmel P
Proc Natl Acad Sci U S A 113 14300-14305 (2016)
PMID: 27911835

Function and Biology Details

Reaction catalysed: 
ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155960 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alanine--tRNA ligase, cytoplasmic Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 23.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4
UniProt:
  • Canonical: P49588 (Residues: 757-965; Coverage: 22%)
Gene names: AARS, AARS1
Sequence domains: DHHA1 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: C2221
Unit cell:
a: 90.829Å b: 136.141Å c: 59.077Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.258
Expression system: Escherichia coli-Pichia pastoris shuttle vector pPpARG4

Quick links

Citations

2 review citations

Emerging mechanisms of aminoacyl-tRNA synthetase mutations in recessive and dominant human disease.
Meyer-Schuman et al. (2017)
1 more

5 mentions without citation

Neurodegenerative Charcot-Marie-Tooth disease as a case study to decipher novel functions of aminoacyl-tRNA synthetases.
Wei et al. (2019)
4 more