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6V2W

Crystal structure of the BRAF:MEK1 kinases in complex with AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0000165biological_processMAPK cascade
B0000187biological_processobsolete activation of MAPK activity
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004708molecular_functionMAP kinase kinase activity
B0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0005078molecular_functionMAP-kinase scaffold activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005769cellular_componentearly endosome
B0005770cellular_componentlate endosome
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005813cellular_componentcentrosome
B0005816cellular_componentspindle pole body
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006468biological_processprotein phosphorylation
B0006935biological_processchemotaxis
B0007165biological_processsignal transduction
B0007507biological_processheart development
B0008285biological_processnegative regulation of cell population proliferation
B0010628biological_processpositive regulation of gene expression
B0014044biological_processSchwann cell development
B0016020cellular_componentmembrane
B0021697biological_processcerebellar cortex formation
B0030182biological_processneuron differentiation
B0030216biological_processkeratinocyte differentiation
B0030295molecular_functionprotein kinase activator activity
B0030878biological_processthyroid gland development
B0032872biological_processregulation of stress-activated MAPK cascade
B0035987biological_processendodermal cell differentiation
B0038133biological_processERBB2-ERBB3 signaling pathway
B0042552biological_processmyelination
B0043410biological_processpositive regulation of MAPK cascade
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0044342biological_processtype B pancreatic cell proliferation
B0045893biological_processpositive regulation of DNA-templated transcription
B0048009biological_processinsulin-like growth factor receptor signaling pathway
B0048538biological_processthymus development
B0048679biological_processregulation of axon regeneration
B0048870biological_processcell motility
B0050772biological_processpositive regulation of axonogenesis
B0060020biological_processBergmann glial cell differentiation
B0060324biological_processface development
B0060425biological_processlung morphogenesis
B0060440biological_processtrachea formation
B0060502biological_processepithelial cell proliferation involved in lung morphogenesis
B0060674biological_processplacenta blood vessel development
B0060711biological_processlabyrinthine layer development
B0070371biological_processERK1 and ERK2 cascade
B0070374biological_processpositive regulation of ERK1 and ERK2 cascade
B0071902biological_processpositive regulation of protein serine/threonine kinase activity
B0090170biological_processregulation of Golgi inheritance
B0090398biological_processcellular senescence
B0097110molecular_functionscaffold protein binding
B0106310molecular_functionprotein serine kinase activity
B1903226biological_processpositive regulation of endodermal cell differentiation
B2000641biological_processregulation of early endosome to late endosome transport
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue ANP A 801
ChainResidue
AILE463
ACYS532
AASP576
ALYS578
AASN581
APHE583
AASP594
AMG802
BGLU102
BASN382
AGLY464
AGLY466
ASER467
AVAL471
AALA481
ALYS483
AGLN530
ATRP531

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 802
ChainResidue
AASN580
AASN581
AASP594
AANP801

site_idAC3
Number of Residues16
Detailsbinding site for residue ANP B 801
ChainResidue
BLEU74
BALA76
BVAL82
BALA95
BLYS97
BMET143
BGLU144
BMET146
BSER150
BGLN153
BLYS192
BSER194
BASN195
BLEU197
BASP208
BMG802

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 802
ChainResidue
BLYS97
BASN195
BASP208
BANP801

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
AILE463-LYS483
BLEU74-LYS97

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKsnNIFL
ChainResidueDetails
AILE572-LEU584
BILE186-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
BASP190

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
BMET143
BSER150
BLYS192
BASP208
BLEU74

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQH
ChainResidueDetails
BLYS97

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:19161339, ECO:0007744|PDB:3EQF
ChainResidueDetails
BSER194
BGLU144

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by anthrax lethal factor
ChainResidueDetails
BPRO8

site_idSWS_FT_FI6
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
BALA218

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by BRAF and RAF1 => ECO:0000269|PubMed:20956560, ECO:0000269|PubMed:29433126, ECO:0000269|PubMed:8131746
ChainResidueDetails
BALA222

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18691976
ChainResidueDetails
BTHR286

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986
ChainResidueDetails
BTHR292

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PAK => ECO:0000269|PubMed:16129686
ChainResidueDetails
BSER298

221051

PDB entries from 2024-06-12

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