› 2wey

X-ray diffraction
2.8Å resolution

Human PDE-papaverine complex obtained by ligand soaking of cross- linked protein crystals

Released:
DOI: 10.2210/pdb2wey/pdb
PDB entry 2wey coloured by chain, front view.
PDB entry 2wey coloured by chain, side view.
PDB entry 2wey coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Cross-linking of protein crystals as an aid in the generation of binary protein-ligand crystal complexes, exemplified by the human PDE10a-papaverine structure.
Andersen OA, Schönfeld DL, Toogood-Johnson I, Felicetti B, Albrecht C, Fryatt T, Whittaker M, Hallett D, Barker J
Acta Crystallogr D Biol Crystallogr 65 872-4 (2009)
PMID: 19622871

Function and Biology Details

Reaction catalysed: 
Nucleoside 3',5'-cyclic phosphate + H(2)O = nucleoside 5'-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195088 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 39.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y233 (Residues: 713-1055; Coverage: 33%)
Gene name: PDE10A
Structure domains: 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain

Ligands and Environments

3 bound ligands:
Ligand EV1 2 x EV1
Ligand ZN 2 x ZN
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 50.84Å b: 81.57Å c: 157.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.239 0.3
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Protein X-ray Crystallography and Drug Discovery.
Maveyraud et al. (2020)
2 more

2 mentions without citation

Guidelines for the successful generation of protein-ligand complex crystals.
Müller I. (2017)
1 more