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3GU7

Crystal structure of DAPKQ23V-ADP-Mg2+

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 Residues25
DetailsBINDING SITE FOR RESIDUE ADP A 296
ChainResidue
ALEU19
AGLU94
AVAL96
AGLU100
AGLU143
AASN144
AMET146
AILE160
AASP161
AMG297
AHOH333
AGLY20
AHOH385
AHOH407
AHOH437
AHOH490
AHOH517
AHOH519
ASER21
AGLY22
AVAL23
AVAL27
AALA40
ALYS42
AILE77

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 297
ChainResidue
AASN144
AASP161
AADP296
AHOH385
AHOH490
AHOH517

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues28
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGVFAVVKkCrekstglqyaak......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 Residues262
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
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_FI3
Number of Residues13
DetailsBinding site: {}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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