› 3itm

X-ray diffraction
2.49Å resolution

Catalytic domain of hPDE2A

Released:
DOI: 10.2210/pdb3itm/pdb
PDB entry 3itm coloured by chain, front view.
PDB entry 3itm coloured by chain, side view.
PDB entry 3itm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanism for the allosteric regulation of phosphodiesterase 2A deduced from the X-ray structure of a near full-length construct.
Pandit J, Forman MD, Fennell KF, Dillman KS, Menniti FS
Proc Natl Acad Sci U S A 106 18225-30 (2009)
PMID: 19828435

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-517247 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cGMP-dependent 3',5'-cyclic phosphodiesterase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 345 amino acids
Theoretical weight: 40.23 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: O00408 (Residues: 579-919; Coverage: 36%)
Gene name: PDE2A
Sequence domains: 3'5'-cyclic nucleotide phosphodiesterase
Structure domains: 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P6122
Unit cell:
a: 108.017Å b: 108.017Å c: 515.563Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.227 0.286
Expression system: Spodoptera frugiperda

Quick links

Citations

26 review citations

cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action.
Francis et al. (2010)
25 more

1 mention without citation

Mechanism for the allosteric regulation of phosphodiesterase 2A deduced from the X-ray structure of a near full-length construct.
Pandit et al. (2009)