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2V92

Crystal structure of the regulatory fragment of mammalian AMPK in complexes with ATP-AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004679molecular_functionAMP-activated protein kinase activity
E0000166molecular_functionnucleotide binding
E0004672molecular_functionprotein kinase activity
E0004679molecular_functionAMP-activated protein kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006629biological_processlipid metabolic process
E0006631biological_processfatty acid metabolic process
E0006633biological_processfatty acid biosynthetic process
E0010628biological_processpositive regulation of gene expression
E0016208molecular_functionAMP binding
E0019887molecular_functionprotein kinase regulator activity
E0019901molecular_functionprotein kinase binding
E0031588cellular_componentnucleotide-activated protein kinase complex
E0031669biological_processcellular response to nutrient levels
E0032991cellular_componentprotein-containing complex
E0043531molecular_functionADP binding
E0044877molecular_functionprotein-containing complex binding
E0051170biological_processimport into nucleus
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ATP E1327
ChainResidue
EARG69
EVAL275
ELEU276
EVAL296
EHIS297
EARG298
EHOH2229
EHOH2230
EHOH2231
EHOH2232
EHOH2233
EARG151
EHOH2234
EHOH2235
ELYS169
EILE239
ESER241
EPHE243
EASP244
EARG268
EGLY274

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ATP E1328
ChainResidue
EARG69
EMET84
ETHR86
EILE87
ETHR88
EASP89
EPRO127
ELEU128
EVAL129
EILE149
EHIS150
EARG151
EPRO153
ESER225
ELYS242
EHOH2036
EHOH2232
EHOH2236
EHOH2237
EHOH2238

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE AMP E1329
ChainResidue
AARG457
EHIS150
ETHR199
EASN202
EILE203
EALA204
EVAL224
ESER225
EALA226
EHIS297
EILE311
ESER313
ESER315
EASP316
EHOH2199
EHOH2239
EHOH2241
EHOH2242

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0007744|PDB:2V92
ChainResidueDetails
EARG69
EMET84
EVAL129
EARG151
ELYS169
ESER241
EARG268
ELEU276

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17851531, ECO:0000269|PubMed:21399626, ECO:0007744|PDB:2V8Q, ECO:0007744|PDB:2Y8L
ChainResidueDetails
EHIS150
ETHR199
EALA204
ESER225
EHIS297
ESER313

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634
ChainResidueDetails
ESER260

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634
ChainResidueDetails
ETHR262

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634
ChainResidueDetails
ESER269

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12764152, ECO:0007744|PubMed:22673903
ChainResidueDetails
AASP496

217705

건을2024-03-27부터공개중

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