3erj

X-ray diffraction
1.8Å resolution

Crystal structure of the peptidyl-tRNA hydrolase AF2095 from Archaeglobus fulgidis. Northeast Structural Genomics Consortium target GR4

Released:
Source organism: Archaeoglobus fulgidus
Entry authors: Forouhar F, Su M, Seetharaman J, Conover K, Janjua H, Xiao R, Cunningham K, Ma L-C, Cooper B, Baran MC, Liu J, Acton TB, Montelione GT, Tong L, Hunt JF, Northeast Structural Genomics Consortium (NESG)

Function and Biology Details

Reaction catalysed:
N-substituted aminoacyl-tRNA + H(2)O = N-substituted amino acid + tRNA
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-127988 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-tRNA hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 123 amino acids
Theoretical weight: 13.58 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O28185 (Residues: 1-115; Coverage: 100%)
Gene names: AF_2095, pth
Sequence domains: Peptidyl-tRNA hydrolase PTH2
Structure domains: Bit1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 43.903Å b: 46.925Å c: 105.263Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.224
Expression system: Escherichia coli