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2YA9

Crystal structure of the autoinhibited form of mouse DAPK2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006468biological_processprotein phosphorylation
A0006915biological_processapoptotic process
A0031410cellular_componentcytoplasmic vesicle
A0034423cellular_componentautophagosome lumen
A0035556biological_processintracellular signal transduction
A0043065biological_processpositive regulation of apoptotic process
A0106310molecular_functionprotein serine kinase activity
A1990266biological_processneutrophil migration
A2001242biological_processregulation of intrinsic apoptotic signaling pathway
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005516molecular_functioncalmodulin binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0006468biological_processprotein phosphorylation
B0006915biological_processapoptotic process
B0031410cellular_componentcytoplasmic vesicle
B0034423cellular_componentautophagosome lumen
B0035556biological_processintracellular signal transduction
B0043065biological_processpositive regulation of apoptotic process
B0106310molecular_functionprotein serine kinase activity
B1990266biological_processneutrophil migration
B2001242biological_processregulation of intrinsic apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE D1D A 1302
ChainResidue
APHE178
AGLY179
AHOH2206
AHOH2207
BILE177
BD1D1302
BHOH2206

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1303
ChainResidue
AHOH2122
BASN190
BHOH2121
BHOH2127
AASN190
AHOH2115

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE D1D B 1302
ChainResidue
AD1D1302
AHOH2206
BPHE178
BGLY179
BHOH2206

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP139
BASP139

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:21497605
ChainResidueDetails
ALEU19
ALYS42
BLEU19
BLYS42

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER289
ASER339
BSER289
BSER339

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:Q9UIK4
ChainResidueDetails
ASER308
BSER308

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q9UIK4
ChainResidueDetails
ATHR359
BTHR359

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PDB entries from 2024-07-31

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