6BG2

Crystal structure of cGMP-dependent protein kinase Ialpha (PKG Ialpha) catalytic domain in AMP-PNP bound state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004692	molecular_function	cGMP-dependent protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004692	molecular_function	cGMP-dependent protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0004692	molecular_function	cGMP-dependent protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0004692	molecular_function	cGMP-dependent protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	binding site for residue ANP C 700

Chain	Residue
C	GLY367
C	GLU439
C	CYS441
C	GLU445
C	LYS486
C	GLU488
C	ASN489
C	ILE491
C	ASP502
C	PHE649
C	MN701
C	GLY369
C	MN702
C	HOH842
C	HOH872
C	HOH907
C	HOH930
C	HOH936
C	GLY370
C	PHE371
C	GLY372
C	VAL374
C	ALA388
C	LYS390
C	MET438

---

site_id	AC2
Number of Residues	4
Details	binding site for residue MN C 701

Chain	Residue
C	ASP502
C	ANP700
C	HOH837
C	HOH1079

---

site_id	AC3
Number of Residues	4
Details	binding site for residue MN C 702

Chain	Residue
C	ASN489
C	ASP502
C	ANP700
C	HOH936

---

site_id	AC4
Number of Residues	25
Details	binding site for residue ANP B 700

Chain	Residue
B	GLY367
B	GLY369
B	GLY370
B	PHE371
B	GLY372
B	VAL374
B	ALA388
B	LYS390
B	GLU439
B	CYS441
B	GLU445
B	LYS486
B	GLU488
B	ASN489
B	ILE491
B	ASP502
B	PHE649
B	MN701
B	MN702
B	HOH830
B	HOH903
B	HOH922
B	HOH937
B	HOH954
B	HOH955

---

site_id	AC5
Number of Residues	4
Details	binding site for residue MN B 701

Chain	Residue
B	ASP502
B	ANP700
B	HOH832
B	HOH1028

---

site_id	AC6
Number of Residues	4
Details	binding site for residue MN B 702

Chain	Residue
B	ASN489
B	ASP502
B	ANP700
B	HOH937

---

site_id	AC7
Number of Residues	20
Details	binding site for residue ANP A 700

Chain	Residue
A	PHE371
A	VAL374
A	ALA388
A	LYS390
A	VAL422
A	MET438
A	GLU439
A	CYS441
A	GLU445
A	VAL501
A	ASP502
A	PHE649
A	MN701
A	MN702
A	HOH825
A	HOH859
A	HOH862
A	HOH863
A	HOH951
A	HOH995

---

site_id	AC8
Number of Residues	4
Details	binding site for residue MN A 701

Chain	Residue
A	ASP502
A	ANP700
A	MN702
A	HOH825

---

site_id	AC9
Number of Residues	5
Details	binding site for residue MN A 702

Chain	Residue
A	ASN489
A	ASP502
A	ANP700
A	MN701
A	HOH995

---

site_id	AD1
Number of Residues	26
Details	binding site for residue ANP D 700

Chain	Residue
D	GLY372
D	VAL374
D	ALA388
D	LYS390
D	GLU439
D	CYS441
D	GLU445
D	LYS486
D	GLU488
D	ASN489
D	ILE491
D	ASP502
D	PHE649
D	MN701
D	MN702
D	HOH848
D	HOH872
D	HOH888
D	HOH910
D	HOH912
D	HOH998
D	HOH1057
D	GLY367
D	GLY369
D	GLY370
D	PHE371

---

site_id	AD2
Number of Residues	4
Details	binding site for residue MN D 701

Chain	Residue
D	ASP502
D	ANP700
D	HOH841
D	HOH1057

---

site_id	AD3
Number of Residues	4
Details	binding site for residue MN D 702

Chain	Residue
D	ASN489
D	ASP502
D	ANP700
D	HOH888

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	25
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGGFGRVElVqlkseeskt.........FAMK

Chain	Residue	Details
C	LEU366-LYS390

---

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKpeNLIL

Chain	Residue	Details
C	ILE480-LEU492

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	36
Details	Compositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P0C605","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24239458","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25271401","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4KU7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QXK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---