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3EQD

X-ray structure of the human mitogen-activated protein kinase kinase 1 (MEK1) in a binary complex with ATP-GS and MG2P

Functional Information from GO Data
ChainGOidnamespacecontents
A0000165biological_processMAPK cascade
A0000166molecular_functionnucleotide binding
A0000187biological_processobsolete activation of MAPK activity
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004708molecular_functionMAP kinase kinase activity
A0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0005078molecular_functionMAP-kinase scaffold activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005769cellular_componentearly endosome
A0005770cellular_componentlate endosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006468biological_processprotein phosphorylation
A0006935biological_processchemotaxis
A0007165biological_processsignal transduction
A0007507biological_processheart development
A0008285biological_processnegative regulation of cell population proliferation
A0010628biological_processpositive regulation of gene expression
A0014044biological_processSchwann cell development
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0021697biological_processcerebellar cortex formation
A0030182biological_processneuron differentiation
A0030216biological_processkeratinocyte differentiation
A0030295molecular_functionprotein kinase activator activity
A0030878biological_processthyroid gland development
A0032872biological_processregulation of stress-activated MAPK cascade
A0035987biological_processendodermal cell differentiation
A0038133biological_processERBB2-ERBB3 signaling pathway
A0042552biological_processmyelination
A0043410biological_processpositive regulation of MAPK cascade
A0043539molecular_functionprotein serine/threonine kinase activator activity
A0044342biological_processtype B pancreatic cell proliferation
A0045893biological_processpositive regulation of DNA-templated transcription
A0048009biological_processinsulin-like growth factor receptor signaling pathway
A0048538biological_processthymus development
A0048679biological_processregulation of axon regeneration
A0048870biological_processcell motility
A0050772biological_processpositive regulation of axonogenesis
A0060020biological_processBergmann glial cell differentiation
A0060324biological_processface development
A0060425biological_processlung morphogenesis
A0060440biological_processtrachea formation
A0060502biological_processepithelial cell proliferation involved in lung morphogenesis
A0060674biological_processplacenta blood vessel development
A0060711biological_processlabyrinthine layer development
A0070371biological_processERK1 and ERK2 cascade
A0070374biological_processpositive regulation of ERK1 and ERK2 cascade
A0071902biological_processpositive regulation of protein serine/threonine kinase activity
A0090170biological_processregulation of Golgi inheritance
A0090398biological_processcellular senescence
A0097110molecular_functionscaffold protein binding
A0106310molecular_functionprotein serine kinase activity
A1903226biological_processpositive regulation of endodermal cell differentiation
A2000641biological_processregulation of early endosome to late endosome transport
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE AGS A 2
ChainResidue
AMG3
AGLU144
AMET146
ASER150
AGLN153
ALYS192
ASER194
AASN195
ALEU197
AASP208
AHOH482
ALEU74
AHOH521
AGLY77
AASN78
AGLY80
AVAL82
AALA95
ALYS97
AMET143

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 3
ChainResidue
AAGS2
AASN195
AASP208
AHOH520
AHOH521

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 5
ChainResidue
AASP65
AASP66
AHOH500

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 6
ChainResidue
AASP65
AASP66
AHOH414
AHOH441
AHOH470
AHOH471

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK
ChainResidueDetails
ALEU74-LYS97

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKpsNILV
ChainResidueDetails
AILE186-VAL198

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
AASP190

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:15543157, ECO:0000269|PubMed:17880056, ECO:0000269|PubMed:18951019, ECO:0000269|PubMed:19019675, ECO:0000269|PubMed:19706763, ECO:0000269|PubMed:21310613
ChainResidueDetails
ALEU74
AMET143
ASER150
ALYS192
AASP208

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQH
ChainResidueDetails
ALYS97

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF
ChainResidueDetails
AGLU144
ASER194

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746
ChainResidueDetails
ASER218

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746
ChainResidueDetails
ASER222

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ATHR286

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986
ChainResidueDetails
ATHR292

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PAK => ECO:0000269|PubMed:16129686
ChainResidueDetails
AASN298

218853

PDB entries from 2024-04-24

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