Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9VHU

Crystal structure of inactive calcium-dependent protein kinase 3 (CPK3) from Arabidopsis thaliana

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000325	cellular_component	plant-type vacuole
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
A	0005515	molecular_function	protein binding
A	0005516	molecular_function	calmodulin binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0009507	cellular_component	chloroplast
A	0009651	biological_process	response to salt stress
A	0009738	biological_process	abscisic acid-activated signaling pathway
A	0009931	molecular_function	calcium-dependent protein serine/threonine kinase activity
A	0010119	biological_process	regulation of stomatal movement
A	0016020	cellular_component	membrane
A	0035556	biological_process	intracellular signal transduction
A	0046777	biological_process	protein autophosphorylation
A	0106310	molecular_function	protein serine kinase activity
B	0000325	cellular_component	plant-type vacuole
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
B	0005515	molecular_function	protein binding
B	0005516	molecular_function	calmodulin binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0009507	cellular_component	chloroplast
B	0009651	biological_process	response to salt stress
B	0009738	biological_process	abscisic acid-activated signaling pathway
B	0009931	molecular_function	calcium-dependent protein serine/threonine kinase activity
B	0010119	biological_process	regulation of stomatal movement
B	0016020	cellular_component	membrane
B	0035556	biological_process	intracellular signal transduction
B	0046777	biological_process	protein autophosphorylation
B	0106310	molecular_function	protein serine kinase activity
C	0000325	cellular_component	plant-type vacuole
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
C	0005515	molecular_function	protein binding
C	0005516	molecular_function	calmodulin binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0009507	cellular_component	chloroplast
C	0009651	biological_process	response to salt stress
C	0009738	biological_process	abscisic acid-activated signaling pathway
C	0009931	molecular_function	calcium-dependent protein serine/threonine kinase activity
C	0010119	biological_process	regulation of stomatal movement
C	0016020	cellular_component	membrane
C	0035556	biological_process	intracellular signal transduction
C	0046777	biological_process	protein autophosphorylation
C	0106310	molecular_function	protein serine kinase activity
D	0000325	cellular_component	plant-type vacuole
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0004683	molecular_function	calcium/calmodulin-dependent protein kinase activity
D	0005515	molecular_function	protein binding
D	0005516	molecular_function	calmodulin binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0009507	cellular_component	chloroplast
D	0009651	biological_process	response to salt stress
D	0009738	biological_process	abscisic acid-activated signaling pathway
D	0009931	molecular_function	calcium-dependent protein serine/threonine kinase activity
D	0010119	biological_process	regulation of stomatal movement
D	0016020	cellular_component	membrane
D	0035556	biological_process	intracellular signal transduction
D	0046777	biological_process	protein autophosphorylation
D	0106310	molecular_function	protein serine kinase activity

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DTDNNGIVTleEL

Chain	Residue	Details
A	ASP392-LEU404
A	ASP428-PHE440
A	ASP464-LEU476
A	ASP499-PHE511

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGQFGVTYlVthketkqq..........VACK

Chain	Residue	Details
A	LEU84-LYS107

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

Chain	Residue	Details
A	VAL198-PHE210

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1032
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	140
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	140
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	136
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	140
Details	Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	120
Details	Region: {"description":"Autoinhibitory domain","evidences":[{"source":"UniProtKB","id":"Q06850","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
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_FI8
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	76
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9FKW4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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