› 1h4v

X-ray diffraction
2.4Å resolution

HISTIDYL-TRNA SYNTHETASE from Thermus Thermophilus (ligand free)

Released:
DOI: 10.2210/pdb1h4v/pdb
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PDB entry 1h4v coloured by chain, front view.
PDB entry 1h4v coloured by chain, side view.
PDB entry 1h4v coloured by chain, top view.
Source organism: Thermus thermophilus HB27
Primary publication:
A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: comparison with histidyl-tRNA synthetase.
Yaremchuk A, Tukalo M, Grøtli M, Cusack S
J Mol Biol 309 989-1002 (2001)
PMID: 11399074

Function and Biology Details

Reaction catalysed: 
ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine--tRNA ligase Chain: B
Molecule details ›
Chain: B
Length: 421 amino acids
Theoretical weight: 47.13 KDa
Source organism: Thermus thermophilus HB27
UniProt:
  • Canonical: P62374 (Residues: 1-421; Coverage: 100%)
Gene names: TT_C0360, hisS
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID2
Spacegroup: C2221
Unit cell:
a: 111.13Å b: 102.15Å c: 91.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.256

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Citations

10 review citations

Implications of protein flexibility for drug discovery.
Teague SJ. (2003)
9 more

3 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
2 more

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