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2XZS

Death associated protein kinase 1 residues 1-312

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1313
ChainResidue
AASN144
AASP161
AHOH2095

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG B 1303
ChainResidue
BASN144
BASP161

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAVVKkCrekstglqyaak......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 Residues10
DetailsBINDING:
ChainResidueDetails
ALEU19
BASP161
ALYS42
AGLU94
AGLU100
AASP161
BLEU19
BLYS42
BGLU94
BGLU100

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by RPS6KA1 and RPS6KA3 => ECO:0000269|PubMed:16213824
ChainResidueDetails
ASER289
BSER289

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:11579085, ECO:0000269|PubMed:15729359, ECO:0000269|PubMed:17056602
ChainResidueDetails
ASER308
BSER308

224004

PDB entries from 2024-08-21

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