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7CCW

Crystal structure of death-associated protein kinase 1 in complex with resveratrol and MES

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue STL A 301
ChainResidue
AGLY20
AMET146
AMES302
AHOH429
ASER21
AGLY22
AALA40
AILE77
AGLU94
ALEU95
AVAL96
AGLU100

site_idAC2
Number of Residues11
Detailsbinding site for residue MES A 302
ChainResidue
AVAL27
ALYS42
AGLU143
AASN144
AILE160
AASP161
ASTL301
ASO4304
AHOH429
AHOH472
AHOH484

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
AARG63
ALYS175
AHOH403
AHOH437

site_idAC4
Number of Residues6
Detailsbinding site for residue SO4 A 304
ChainResidue
AGLY22
AGLN23
AMES302
AHOH412
AHOH432
AHOH581

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 305
ChainResidue
ALYS86
AARG253
AHOH509

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP139

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ALEU19
ALYS42
AGLU94
AGLU100
AASP161

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PDB entries from 2024-07-31

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