1oni

X-ray diffraction
1.9Å resolution

Crystal structure of a human p14.5, a translational inhibitor reveals different mode of ligand binding near the invariant residues of the Yjgf/UK114 protein family

Released:

Function and Biology Details

Reaction catalysed:
2-iminobutanoate + H(2)O = 2-oxobutanoate + NH(3)
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-156631 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-iminobutanoate/2-iminopropanoate deaminase Chains: A, B, C, D, E, F, G, H, I
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I
Length: 138 amino acids
Theoretical weight: 14.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P52758 (Residues: 2-137; Coverage: 99%)
Gene names: HRSP12, RIDA
Sequence domains: Endoribonuclease L-PSP
Structure domains: RutC-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P3121
Unit cell:
a: 154.158Å b: 154.158Å c: 104.559Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.185 0.185 0.216
Expression system: Escherichia coli