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2YA3

STRUCTURE OF THE REGULATORY FRAGMENT OF MAMMALIAN AMPK IN COMPLEX WITH COUMARIN ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004679molecular_functionAMP-activated protein kinase activity
E0004672molecular_functionprotein kinase activity
E0004679molecular_functionAMP-activated protein kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
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 Residues17
DetailsBINDING SITE FOR RESIDUE J7V E 1325
ChainResidue
EMET84
EVAL129
EILE149
EHIS150
EARG151
EPRO153
ELYS242
EHOH2014
EHOH2018
ETHR86
ETHR88
EASP89
EASN92
EARG96
ETYR120
ELYS126
ELEU128

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE J7V E 1326
ChainResidue
EARG69
ELYS169
ESER225
ESER241
ELYS242
EPHE243
EGLY274
EVAL275
ELEU276
EVAL296
EHIS297
EARG298
EHOH2066
EHOH2087
EHOH2088

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE AMP E 1327
ChainResidue
AARG457
EHIS150
ETHR199
EILE203
EALA204
EVAL224
ESER225
EALA226
EHIS297
EILE311
ESER313
ESER315
EASP316
EHOH2089
EHOH2090

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

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건을2024-09-18부터공개중

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