Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2W2C

STRUCTURE OF THE TETRADECAMERIC OLIGOMERISATION DOMAIN OF CALCIUM- CALMODULIN DEPENDENT PROTEIN KINASE II DELTA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
A	0005516	molecular_function	calmodulin binding
A	0006468	biological_process	protein phosphorylation
B	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
B	0005516	molecular_function	calmodulin binding
B	0006468	biological_process	protein phosphorylation
C	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
C	0005516	molecular_function	calmodulin binding
C	0006468	biological_process	protein phosphorylation
D	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
D	0005516	molecular_function	calmodulin binding
D	0006468	biological_process	protein phosphorylation
E	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
E	0005516	molecular_function	calmodulin binding
E	0006468	biological_process	protein phosphorylation
F	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
F	0005516	molecular_function	calmodulin binding
F	0006468	biological_process	protein phosphorylation
G	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
G	0005516	molecular_function	calmodulin binding
G	0006468	biological_process	protein phosphorylation
H	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
H	0005516	molecular_function	calmodulin binding
H	0006468	biological_process	protein phosphorylation
I	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
I	0005516	molecular_function	calmodulin binding
I	0006468	biological_process	protein phosphorylation
J	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
J	0005516	molecular_function	calmodulin binding
J	0006468	biological_process	protein phosphorylation
K	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
K	0005516	molecular_function	calmodulin binding
K	0006468	biological_process	protein phosphorylation
L	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
L	0005516	molecular_function	calmodulin binding
L	0006468	biological_process	protein phosphorylation
M	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
M	0005516	molecular_function	calmodulin binding
M	0006468	biological_process	protein phosphorylation
N	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
N	0005516	molecular_function	calmodulin binding
N	0006468	biological_process	protein phosphorylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT A 632

Chain	Residue
A	ILE361
A	TYR369
A	ARG433
A	ARG453
A	PHE467
A	ARG469

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT B 632

Chain	Residue
B	ARG453
B	PHE467
B	ARG469
B	ILE361
B	TYR369
B	ARG433

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT C 632

Chain	Residue
C	ILE361
C	TYR369
C	ARG433
C	ARG453
C	PHE467
C	ARG469

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT D 632

Chain	Residue
D	ILE361
D	TYR369
D	ARG433
D	ARG453
D	PHE467
D	ARG469

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT E 632

Chain	Residue
E	ILE361
E	TYR369
E	ARG453
E	PHE467
E	ARG469

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT F 632

Chain	Residue
F	ILE361
F	TYR369
F	ARG453
F	PHE467
F	ARG469

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT G 632

Chain	Residue
G	ILE361
G	TYR369
G	ARG433
G	ARG453
G	PHE467
G	ARG469

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ACT H 632

Chain	Residue
H	ILE361
H	TYR369
H	ARG453
H	PHE467
H	ARG469

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT I 632

Chain	Residue
I	ILE361
I	TYR369
I	ARG433
I	ARG453
I	PHE467
I	ARG469

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT J 632

Chain	Residue
J	ILE361
J	TYR369
J	ARG433
J	ARG453
J	PHE467
J	ARG469

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT K 632

Chain	Residue
K	ILE361
K	TYR369
K	ARG453
K	PHE467
K	ARG469
K	HOH2001

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT L 632

Chain	Residue
L	ILE361
L	TYR369
L	ARG433
L	ARG453
L	PHE467
L	ARG469

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT M 632

Chain	Residue
M	ILE361
M	TYR369
M	ARG433
M	ARG453
M	PHE467
M	ARG469

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT N 632

Chain	Residue
N	ILE361
N	TYR369
N	ARG433
N	ARG453
N	PHE467
N	ARG469

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD B 1472

Chain	Residue
B	ASP425
B	HOH2006
B	HOH2009
L	ASP425

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD H 1472

Chain	Residue
H	ASP424
N	ASP425
N	ARG457

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD F 1472

Chain	Residue
F	ASP425
G	ASP425
G	HOH2005

site_id	BC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CD J 1472

Chain	Residue
J	ASP425
J	CD1474
M	ASP425

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CD J 1473

Chain	Residue
G	ASP424
J	ASP424

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CD J 1474

Chain	Residue
M	ASP425
J	ASP424
J	ASP425
J	CD1472

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q6PHZ2","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)