› 1tbb

X-ray diffraction
1.6Å resolution

Catalytic Domain Of Human Phosphodiesterase 4D In Complex With Rolipram

Released:
DOI: 10.2210/pdb1tbb/pdb
PDB entry 1tbb coloured by chain, front view.
PDB entry 1tbb coloured by chain, side view.
PDB entry 1tbb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A glutamine switch mechanism for nucleotide selectivity by phosphodiesterases.
Zhang KY, Card GL, Suzuki Y, Artis DR, Fong D, Gillette S, Hsieh D, Neiman J, West BL, Zhang C, Milburn MV, Kim SH, Schlessinger J, Bollag G
Mol Cell 15 279-86 (2004)
PMID: 15260978

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3',5'-cyclic-AMP phosphodiesterase 4D Chains: A, B
Molecule details ›
Chains: A, B
Length: 332 amino acids
Theoretical weight: 38.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08499 (Residues: 388-715; Coverage: 41%)
Gene names: DPDE3, PDE4D
Sequence domains: 3'5'-cyclic nucleotide phosphodiesterase
Structure domains: 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain

Ligands and Environments

4 bound ligands:
Ligand ZN 2 x ZN
Ligand MG 2 x MG
Ligand ROL 2 x ROL
Ligand EDO 14 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 60.106Å b: 79.019Å c: 164.548Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.204
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Biochemistry and physiology of cyclic nucleotide phosphodiesterases: essential components in cyclic nucleotide signaling.
Conti et al. (2007)
18 more