Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
20A 1-ethyl-N-(phenylmethyl)-4-(tetrahydro-2h-pyran-4-ylamino)-1h-pyrazolo[3,4-B]pyridine-5-carboxamide
ARS Arsenic
MG Magnesium ion
ZN Zinc ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 3D3P   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of PDE4B catalytic domain in complex with a pyrazolopyridine inhibitor
Release Data : 2009-05-19
Compound :
mol_id molecule chains synonym
1 cAMP-specific 3',5'-cyclic phosphodiesterase 4B A DPDE4, PDE32
ec: 3.1.4.17
fragment: Catalytic domain, residues 324-675
mutation: S654A, S659A, S661A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Spodoptera frugiperda  (taxid:7108)
gene: PDE4B, DPDE4
expression_system_vector_type: BACULOVIRUS
Authors : Somers, D.O., Neu, M.
Keywords : PDE, PHOSPHODIESTERASE, cAMP, Alternative splicing, Hydrolase, Phosphoprotein, Polymorphism
Exp. method : X-RAY DIFFRACTION ( 1.750 Å )
Citation :

Pyrazolopyridines as a novel structural class of potent and selective PDE4 inhibitors.

Hamblin, J.N.,Angell, T.D.,Ballantine, S.P.  et al.
(2008)  Bioorg.Med.Chem.Lett.  18 : 4237 - 4241

PubMed: 18539455
DOI: 10.1016/j.bmcl.2008.05.052

Chain : A
UniProt : Q07343 (PDE4B_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
3',5'-cyclic AMP + H2O = AMP + H(+) 3.1.4.53 PubMed:15260978, PubMed:17519386, PubMed:8392015, PubMed:9371714
left-to-right
Cofactor: Evidence: Note:
Zn(2+) ECO:0000269 | PubMed:10846163
ECO:0000269 | PubMed:15003452
Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions.
Mn(2+) ECO:0000269 | PubMed:10846163
ECO:0000269 | PubMed:15003452
ECO:0000269 | PubMed:15003452
Binds 2 divalent metal cations per subunit. Site 2 has a preference for magnesium and/or manganese ions.