3DYN

human phosphodiestrase 9 in complex with cGMP (Zn inhibited)

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 ZN A 901

Chain	Residue
A	HIS256
A	HIS292
A	ASP293
A	ASP402
A	HOH1000
A	HOH1001

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 902

Chain	Residue
A	HOH1003
A	HOH1004
A	ASP293
A	HOH1000
A	HOH1002

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 901

Chain	Residue
B	HIS256
B	HIS292
B	ASP293
B	ASP402
B	HOH904

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 902

Chain	Residue
B	ASP293
B	HOH904
B	HOH905
B	HOH906
B	HOH907

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE PCG A 903

Chain	Residue
A	HIS252
A	MET365
A	ILE403
A	LEU420
A	TYR424
A	ALA452
A	GLN453
A	PHE456
A	HOH1000
A	HOH1001
A	HOH1017
A	HOH1050
A	HOH1064
A	HOH1070
A	HOH1112
A	HOH1133
A	HOH1196

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE IBM B 903

Chain	Residue
A	ALA499
A	LEU503
B	LEU420
B	TYR424
B	ALA452
B	GLN453
B	PHE456

---

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE PCG B 900

Chain	Residue
B	HIS252
B	HIS256
B	ASP293
B	MET365
B	ASP402
B	ILE403
B	LEU420
B	TYR424
B	ALA452
B	GLN453
B	PHE456
B	HOH904
B	HOH905
B	HOH913
B	HOH918
B	HOH933
B	HOH946
B	HOH994

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	HIS292-TYR303

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18757755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19919087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20121115","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21483814","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22985069","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23025719","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HD1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2YY2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DYN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3JSW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K3E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3K3H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3N3Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4E90","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G2J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G2L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4GH6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8QZV1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---