1r0v

X-ray diffraction
2Å resolution

Structure Determination of the Dimeric Endonuclease in a Pseudo-face-centerd P21212 space group

Released:
Primary publication:
Structure determination of a truncated dimeric splicing endonuclease in pseudo-face-centered space group P2(1)2(1)2.
Acta Crystallogr D Biol Crystallogr 60 447-52 (2004)
PMID: 14993668

Function and Biology Details

Reaction catalysed:
PretRNA = a 3'-half-tRNA molecule with a 5'-OH end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl terminus
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-128117 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA-splicing endonuclease Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 305 amino acids
Theoretical weight: 36 KDa
Source organism: Archaeoglobus fulgidus DSM 4304
Expression system: Escherichia coli
UniProt:
  • Canonical: O29362 (Residues: 1-305; Coverage: 100%)
Gene names: AF_0900, endA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21212
Unit cell:
a: 128.119Å b: 144.149Å c: 52.385Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.242
Expression system: Escherichia coli