PDBe 2xri

X-ray diffraction
2.15Å resolution

Crystal structure of human ERI1 exoribonuclease 3

Released:
Source organism: Homo sapiens
Entry authors: Welin M, Siponen MI, Arrowsmith CH, Berglund H, Bountra C, Collins R, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Johansson I, Karlberg T, Kol S, Kotenyova T, Kouznetsova E, Moche M, Nyman T, Persson C, Schuler H, Schutz P, Thorsell AG, Tresaugues L, Van Der Berg S, Wahlberg E, Weigelt J, Nordlund P

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ERI1 exoribonuclease 3 Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 25.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O43414 (Residues: 137-337; Coverage: 60%)
  • Best match: O43414-3 (Residues: 1-128)
Gene names: ERI3, PINT1, PRNPIP, PRNPIP1
Sequence domains: Exonuclease
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I222
Unit cell:
a: 68.72Å b: 76.9Å c: 86.98Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.21
Expression system: Escherichia coli BL21(DE3)