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2YAA

Crystal structure of the autoinhibited form of mouse DAPK2 in complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0031410cellular_componentcytoplasmic vesicle
A0034423cellular_componentautophagosome lumen
A0035556biological_processintracellular signal transduction
A0042802molecular_functionidentical protein binding
A0043065biological_processpositive regulation of apoptotic process
A0043231cellular_componentintracellular membrane-bounded organelle
A0043276biological_processanoikis
A0090023biological_processpositive regulation of neutrophil chemotaxis
A0106310molecular_functionprotein serine kinase activity
A1990266biological_processneutrophil migration
A2000424biological_processpositive regulation of eosinophil chemotaxis
A2001242biological_processregulation of intrinsic apoptotic signaling pathway
B0000166molecular_functionnucleotide binding
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005516molecular_functioncalmodulin binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0031410cellular_componentcytoplasmic vesicle
B0034423cellular_componentautophagosome lumen
B0035556biological_processintracellular signal transduction
B0042802molecular_functionidentical protein binding
B0043065biological_processpositive regulation of apoptotic process
B0043231cellular_componentintracellular membrane-bounded organelle
B0043276biological_processanoikis
B0090023biological_processpositive regulation of neutrophil chemotaxis
B0106310molecular_functionprotein serine kinase activity
B1990266biological_processneutrophil migration
B2000424biological_processpositive regulation of eosinophil chemotaxis
B2001242biological_processregulation of intrinsic apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP A 1302
ChainResidue
ALEU19
AASP139
AILE160
AASP161
AHOH2075
AHOH2082
AHOH2182
AGLY22
AGLN23
AALA25
AVAL27
AALA40
ALYS42
AGLU94
AVAL96

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1303
ChainResidue
ASER49
AARG50

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1304
ChainResidue
AASN190
AHOH2103
AHOH2106
AHOH2109
BASN190
BHOH2107

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP B 1302
ChainResidue
BLEU19
BGLY20
BSER21
BGLY22
BPHE24
BVAL27
BALA40
BLYS42
BGLU94
BVAL96
BGLU100
BASN144
BASP161
BHOH2079
BHOH2166
BHOH2167
BHOH2169
BHOH2170

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 B 1303
ChainResidue
AGLN299
BARG50

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAIVKkCrekstgleyaak......FIKK
ChainResidueDetails
ALEU19-LYS46

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IaHfDLKpeNIML
ChainResidueDetails
AILE135-LEU147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues524
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsRegion: {"description":"Autoinhibitory domain"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
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_FI4
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21497605","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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