Brand  (β version)

PDB ID: 1XOZ

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Ligands
Code Name Style Show Link
CIA 6-benzo[1,3]dioxol-5-yl-2-methyl-2,3,6,7,12,12a-hexahydro-pyrazino[1',2':1,6]pyrido[3,4-B]indole-1,4-dione PoSSuM
MG Magnesium ion PoSSuM
ZN Zinc ion PoSSuM
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Structure summary

Code : 1XOZ   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Catalytic Domain Of Human Phosphodiesterase 5A In Complex With Tadalafil
Release Data : 2004-12-14
Compound :
mol_id molecule chains synonym
1 cGMP-specific 3',5'-cyclic phosphodiesterase A CGB-PDE, cGMP-binding cGMP-specific phosphodiesterase, PDE5A
ec: 3.1.4.17
fragment: CATALYTIC DOMAIN OF HUMAN PHOSPHODIESTERASE 5A
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: PDE5A, PDE5
expression_system_strain: BL21(DE3)Codon Plus(RIL)
expression_system_vector_type: PLASMID
expression_system_plasmid: pET15b
Authors : Card, G.L., England, B.P., Suzuki, Y., Fong, D., Powell, B., Lee, B., Luu, C., Tabrizizad, M., Gillette, S., Ibrahim, P.N., Artis, D.R., Bollag, G., Milburn, M.V., Kim, S.-H., Schlessinger, J., Zhang, K.Y.J.
Keywords : Phosphodiesterase, PDE, PDE5A, Tadalafil, Cialis, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.37 Å )
Citation :

Structural Basis for the Activity of Drugs that Inhibit Phosphodiesterases.

Card, G.L.,England, B.P.,Suzuki, Y.  et al.
(2004)  STRUCTURE  12 : 2233 - 2247

PubMed: 15576036
DOI: 10.1016/j.str.2004.10.004

Reaction

Chain : A
UniProt : O76074 (PDE5A_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
3',5'-cyclic GMP + H2O = GMP + H(+) 3.1.4.35 PubMed:15260978, PubMed:9714779
left-to-right PubMed:15260978
Cofactor: Evidence: Note:
Zn(2+) ECO:0000269 | PubMed:12955149
ECO:0000269 | PubMed:15260978
Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc.
Mg(2+) ECO:0000269 | PubMed:12955149
Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc.