2q3s

X-ray diffraction
2.1Å resolution

Ensemble refinement of the protein crystal structure of gene product from Arabidopsis thaliana At5g06450

Released:

Function and Biology Details

Reaction catalysed:
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-190358 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein RISC-INTERACTING CLEARING 3'-5' EXORIBONUCLEASE 2 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 206 amino acids
Theoretical weight: 23.24 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9FNG3 (Residues: 2-206; Coverage: 100%)
Gene names: At5g06450, DECP, MHF15.3, RICE2
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 120.831Å b: 120.831Å c: 185.222Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.155 0.155 0.221
Expression system: Escherichia coli