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2OOY

Crystal structure of the adenylate sensor from AMP-activated protein kinase complexed with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006357biological_processregulation of transcription by RNA polymerase II
E0007165biological_processsignal transduction
E0010514biological_processinduction of conjugation with cellular fusion
E0016208molecular_functionAMP binding
E0019887molecular_functionprotein kinase regulator activity
E0019901molecular_functionprotein kinase binding
E0030295molecular_functionprotein kinase activator activity
E0031588cellular_componentnucleotide-activated protein kinase complex
E0043531molecular_functionADP binding
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006357biological_processregulation of transcription by RNA polymerase II
G0007165biological_processsignal transduction
G0010514biological_processinduction of conjugation with cellular fusion
G0016208molecular_functionAMP binding
G0019887molecular_functionprotein kinase regulator activity
G0019901molecular_functionprotein kinase binding
G0030295molecular_functionprotein kinase activator activity
G0031588cellular_componentnucleotide-activated protein kinase complex
G0043531molecular_functionADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FLC E 402
ChainResidue
DASP250
EHOH495
DGLN251
EVAL56
EARG142
ETHR162
EARG165
EARG287
EHOH460
EHOH489

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ATP E 401
ChainResidue
EARG141
EGLN163
ETHR191
ELEU195
EALA196
EASN215
EILE216
ESER217
EPRO220
EHIS289
EARG290
EILE303
ESER305
ELEU306
EALA307
EASP308
EHOH509
EHOH520
EHOH527

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP G 401
ChainResidue
GARG141
GTHR191
GASN194
GLEU195
GALA196
GASN215
GILE216
GSER217
GALA218
GPRO220
GARG290
GILE303
GSER305
GLEU306
GALA307
GASP308
GHOH520

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2QR1
ChainResidueDetails
GILE35
GARG142
GTHR162
GARG287
EILE35
EARG142
ETHR162
EARG287

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:17289942, ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2OOY
ChainResidueDetails
GARG141
GARG290
EARG141
EARG290

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOY
ChainResidueDetails
GTHR191
GALA196
GSER217
GILE303
ETHR191
EALA196
ESER217
EILE303

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17289942, ECO:0007744|PDB:2OOX
ChainResidueDetails
GSER305
ESER305

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PDB entries from 2024-08-07

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