3v34

X-ray diffraction
2Å resolution

Crystal structure of MCPIP1 conserved domain with magnesium ion in the catalytic center

Released:
Source organism: Homo sapiens
Primary publication:
Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase.
Nucleic Acids Res 40 6957-65 (2012)
PMID: 22561375

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-176962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoribonuclease ZC3H12A Chains: A, B
Molecule details ›
Chains: A, B
Length: 185 amino acids
Theoretical weight: 21.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5D1E8 (Residues: 112-296; Coverage: 31%)
Gene names: MCPIP, MCPIP1, ZC3H12A
Sequence domains: Zc3h12a-like Ribonuclease NYN domain
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P41
Unit cell:
a: 56.349Å b: 56.349Å c: 113.574Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.24
Expression system: Escherichia coli