› 3evi

X-ray diffraction
2.7Å resolution

Crystal structure of the thioredoxin-fold domain of human phosducin-like protein 2

Released:
DOI: 10.2210/pdb3evi/pdb
PDB entry 3evi coloured by chain, front view.
PDB entry 3evi coloured by chain, side view.
PDB entry 3evi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the thioredoxin-fold domain of human phosducin-like protein 2.
Lou X, Bao R, Zhou CZ, Chen Y
Acta Crystallogr Sect F Struct Biol Cryst Commun 65 67-70 (2009)
PMID: 19193988

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185386 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosducin-like protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 118 amino acids
Theoretical weight: 13.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8N4E4 (Residues: 88-205; Coverage: 49%)
Gene name: PDCL2
Sequence domains: Phosducin
Structure domains: Glutaredoxin

Ligands and Environments

2 bound ligands:
Ligand PEG 2 x PEG
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P31
Unit cell:
a: 44.594Å b: 44.594Å c: 141.971Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.234 0.276
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Yeast phosducin-like protein 2 acts as a stimulatory co-factor for the folding of actin by the chaperonin CCT via a ternary complex.
McCormack et al. (2009)
3 more

5 mentions without citation

Structure of the thioredoxin-fold domain of human phosducin-like protein 2.
Lou et al. (2009)
4 more