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7JUR

Crystal Structure of KSR2:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor Trametinib

Functional Information from GO Data
ChainGOidnamespacecontents
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
C0000165biological_processMAPK cascade
C0000166molecular_functionnucleotide binding
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004708molecular_functionMAP kinase kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005769cellular_componentearly endosome
C0005770cellular_componentlate endosome
C0005813cellular_componentcentrosome
C0005856cellular_componentcytoskeleton
C0005925cellular_componentfocal adhesion
C0006468biological_processprotein phosphorylation
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
C0016740molecular_functiontransferase activity
C0032872biological_processregulation of stress-activated MAPK cascade
C0090170biological_processregulation of Golgi inheritance
C0106310molecular_functionprotein serine kinase activity
C2000641biological_processregulation of early endosome to late endosome transport
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGNGGVVFkVshkpsglv..........MARK
ChainResidueDetails
CLEU74-LYS97

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHkDLKskNVFY
ChainResidueDetails
BILE782-TYR794
CILE186-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
CASP190

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:21441910
ChainResidueDetails
CLEU74
CLYS97

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by RAF => ECO:0000269|PubMed:8157000
ChainResidueDetails
CSER218
CSER222

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q02750
ChainResidueDetails
CTHR286

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by MAPK1 => ECO:0000250|UniProtKB:Q01986
ChainResidueDetails
CTHR292

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PAK => ECO:0000250|UniProtKB:Q02750
ChainResidueDetails
CSER298

218853

PDB entries from 2024-04-24

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