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2YAB

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

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 Residues17
DetailsBINDING SITE FOR RESIDUE AMP A 1302
ChainResidue
ALEU19
AILE160
AASP161
AHOH2171
AHOH2345
AHOH2346
AHOH2347
AHOH2348
AHOH2349
AGLY20
ASER21
AALA25
AVAL27
AALA40
ALYS42
AGLU94
AVAL96

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 1303
ChainResidue
AARG271

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1304
ChainResidue
AASN190
AHOH2222
AHOH2225
BASN190
BHOH2226
BHOH2232

site_idAC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP B 1302
ChainResidue
BLEU19
BGLY20
BSER21
BVAL27
BALA40
BLYS42
BILE77
BGLU94
BVAL96
BGLU100
BASN144
BASP161
BHOH2041
BHOH2326
BHOH2327
BHOH2328
BHOH2329
BHOH2330

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1303
ChainResidue
BLYS108
BGLU109
BSER110
BHOH2155

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1304
ChainResidue
AGLN299
BSER49
BARG50
BHOH2331
BHOH2332

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1305
ChainResidue
ALYS222
BARG47
BHOH2097
BHOH2333
BHOH2334
BHOH2335

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1306
ChainResidue
AARG47
AHOH2072
BLYS222
BHOH2337

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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