4OEX

Crystal structure of the PDE5A1 catalytic domain in complex with novel inhibitors

Replaces:  3TSE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004114	molecular_function	3',5'-cyclic-nucleotide phosphodiesterase activity
A	0007165	biological_process	signal transduction
A	0008081	molecular_function	phosphoric diester hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE 5EO A 901

Chain	Residue
A	ARG667
A	ALA779
A	VAL782
A	PHE786
A	GLN817
A	PHE820
A	ILE824
A	HOH1089
A	HOH1154

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ZN A 902

Chain	Residue
A	HIS617
A	HIS653
A	ASP654
A	ASP764
A	HOH1002
A	HOH1003

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 903

Chain	Residue
A	ASP654
A	HOH1002
A	HOH1004
A	HOH1086
A	HOH1093
A	HOH1115

---

Functional Information from PROSITE/UniProt

site_id	PS00126
Number of Residues	12
Details	PDEASE_I_1 3'5'-cyclic nucleotide phosphodiesterase domain signature. HDLdHrGvnNsY

Chain	Residue	Details
A	HIS653-TYR664

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O76083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12955149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15260978","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T9R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1T9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TBF","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"12955149","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---