2OUR

crystal structure of PDE10A2 mutant D674A in complex with cAMP

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
B	0004114	molecular_function	3',5'-cyclic-nucleotide phosphodiesterase activity
B	0007165	biological_process	signal transduction
B	0008081	molecular_function	phosphoric diester hydrolase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 777

Chain	Residue
A	HOH1
A	HOH2
A	HOH3
A	HOH4
A	HOH5
A	ASP564

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 777

Chain	Residue
B	HOH14
B	HOH15
B	ASP564
B	HOH11
B	HOH12
B	HOH13

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE CMP A 778

Chain	Residue
A	HOH1
A	HOH7
A	HOH8
A	HOH9
A	HOH10
A	HOH301
A	HIS525
A	LEU635
A	LEU675
A	ILE692
A	PHE696
A	GLN726
A	PHE729
B	LEU706

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	HIS563-TYR574

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	317
Details	Domain: {"description":"PDEase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01192","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O76083","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17389385","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---