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9VHW

Calcium-bound structure of calcium-dependent protein kinase 3 (CPK3) from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0000325cellular_componentplant-type vacuole
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004683molecular_functioncalcium/calmodulin-dependent protein kinase activity
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009507cellular_componentchloroplast
A0009651biological_processresponse to salt stress
A0009738biological_processabscisic acid-activated signaling pathway
A0009931molecular_functioncalcium-dependent protein serine/threonine kinase activity
A0010119biological_processregulation of stomatal movement
A0016020cellular_componentmembrane
A0035556biological_processintracellular signal transduction
A0046777biological_processprotein autophosphorylation
A0106310molecular_functionprotein serine kinase activity
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DTDNNGIVTleEL
ChainResidueDetails
AASP392-LEU404
AASP428-PHE440
AASP464-LEU476
AASP499-PHE511

site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGQFGVTYlVthketkqq..........VACK
ChainResidueDetails
ALEU84-LYS107

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VmHrDLKpeNFLF
ChainResidueDetails
AVAL198-PHE210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues258
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues34
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues35
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues30
DetailsRegion: {"description":"Autoinhibitory domain","evidences":[{"source":"UniProtKB","id":"Q06850","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues19
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9FKW4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

257179

PDB entries from 2026-07-29

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