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4CFH

Structure of an active form of mammalian AMPK

Replaces:  2Y94
Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
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 Residues12
DetailsBINDING SITE FOR RESIDUE AMP E 1325
ChainResidue
EARG69
EVAL296
EHIS297
EARG298
ELYS169
EILE239
ESER241
EPHE243
EASP244
EARG268
EVAL275
ELEU276

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AMP E 1326
ChainResidue
EHIS150
ETHR199
EILE203
EALA204
EVAL224
ESER225
EALA226
EHIS297
EILE311
ESER313
ESER315
EASP316

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE STU A 1550
ChainResidue
ALEU22
AGLY23
AVAL24
AGLY25
AALA43
ALYS45
AMET93
AGLU94
ATYR95
AVAL96
AGLY99
AGLU100
AGLU143
AASN144
ALEU146
AASP157

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK
ChainResidueDetails
ALEU22-LYS45

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL
ChainResidueDetails
AVAL135-LEU147

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
ATHR344
ATHR371

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 Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q13131
ChainResidueDetails
ASER345
ASER456

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ULK1 => ECO:0000305|PubMed:21460634
ChainResidueDetails
ASER349

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by ULK1 => ECO:0000305|PubMed:21460634
ChainResidueDetails
ATHR357

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:21460634
ChainResidueDetails
ASER386

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건을2024-03-27부터공개중

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