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3GU5

Crystal structure of DAPKQ23V-AMPPNP-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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 296
ChainResidue
AASN144
AASP161
AANP297
AHOH299
AHOH563

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ANP A 297
ChainResidue
AVAL27
AALA40
ALYS42
AILE77
AGLU94
AVAL96
AGLU100
AGLU143
AASN144
AMET146
AILE160
AASP161
AMG296
AHOH298
AHOH299
AHOH300
AHOH383
AHOH450
AHOH453
AHOH472
AHOH563
ALEU19
AGLY20
ASER21
AGLY22

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 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 2024-07-24

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