› 3v32

X-ray diffraction
2Å resolution

Crystal structure of MCPIP1 N-terminal conserved domain

Released:
DOI: 10.2210/pdb3v32/pdb
PDB entry 3v32 coloured by chain, front view.
PDB entry 3v32 coloured by chain, side view.
PDB entry 3v32 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural study of MCPIP1 N-terminal conserved domain reveals a PIN-like RNase.
Xu J, Peng W, Sun Y, Wang X, Xu Y, Li X, Gao G, Rao Z
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
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P41
Unit cell:
a: 56.35Å b: 56.35Å c: 113.238Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.202 0.244
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Post-transcriptional regulatory networks in immunity.
Ivanov et al. (2013)
16 more

5 mentions without citation

Structural conservation of the PIN domain active site across all domains of life.
Senissar et al. (2017)
4 more