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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8U1L

Cryo-EM structure of the RAF1-HSP90-CDC37 complex in the closed state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0016887molecular_functionATP hydrolysis activity
A0046872molecular_functionmetal ion binding
A0051082molecular_functionunfolded protein binding
A0101031cellular_componentprotein folding chaperone complex
A0140662molecular_functionATP-dependent protein folding chaperone
B0000166molecular_functionnucleotide binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0046872molecular_functionmetal ion binding
B0051082molecular_functionunfolded protein binding
B0101031cellular_componentprotein folding chaperone complex
B0140662molecular_functionATP-dependent protein folding chaperone
C0000165biological_processMAPK cascade
C0000166molecular_functionnucleotide binding
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004709molecular_functionMAP kinase kinase kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005741cellular_componentmitochondrial outer membrane
C0005794cellular_componentGolgi apparatus
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006468biological_processprotein phosphorylation
C0006915biological_processapoptotic process
C0007165biological_processsignal transduction
C0007528biological_processneuromuscular junction development
C0008270molecular_functionzinc ion binding
C0008285biological_processnegative regulation of cell population proliferation
C0008286biological_processinsulin receptor signaling pathway
C0010856molecular_functionadenylate cyclase activator activity
C0014044biological_processSchwann cell development
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0019899molecular_functionenzyme binding
C0031143cellular_componentpseudopodium
C0031267molecular_functionsmall GTPase binding
C0031333biological_processnegative regulation of protein-containing complex assembly
C0033138biological_processpositive regulation of peptidyl-serine phosphorylation
C0035023biological_processregulation of Rho protein signal transduction
C0038127biological_processERBB signaling pathway
C0038133biological_processERBB2-ERBB3 signaling pathway
C0042060biological_processwound healing
C0042552biological_processmyelination
C0042802molecular_functionidentical protein binding
C0042981biological_processregulation of apoptotic process
C0043066biological_processnegative regulation of apoptotic process
C0043410biological_processpositive regulation of MAPK cascade
C0045595biological_processregulation of cell differentiation
C0046872molecular_functionmetal ion binding
C0048009biological_processinsulin-like growth factor receptor signaling pathway
C0060333biological_processtype II interferon-mediated signaling pathway
C0106310molecular_functionprotein serine kinase activity
D0000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006457biological_processprotein folding
D0006605biological_processprotein targeting
D0010608biological_processpost-transcriptional regulation of gene expression
D0019887molecular_functionprotein kinase regulator activity
D0019900molecular_functionkinase binding
D0019901molecular_functionprotein kinase binding
D0031072molecular_functionheat shock protein binding
D0050821biological_processprotein stabilization
D0051082molecular_functionunfolded protein binding
D0051087molecular_functionprotein-folding chaperone binding
D0051879molecular_functionHsp90 protein binding
D0060334biological_processregulation of type II interferon-mediated signaling pathway
D0060338biological_processregulation of type I interferon-mediated signaling pathway
D0070062cellular_componentextracellular exosome
D0097110molecular_functionscaffold protein binding
D0101031cellular_componentprotein folding chaperone complex
D1905091biological_processpositive regulation of type 2 mitophagy
D1990565cellular_componentHSP90-CDC37 chaperone complex
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
CILE355-LYS375
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKsnNIFL
ChainResidueDetails
CILE464-LEU476
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR33-GLU42
site_idPS00479
Number of Residues46
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HnFarktflklaf.CdiCqkfLlngfr.....CqtCgykfHehCstkvptm..C
ChainResidueDetails
CHIS139-CYS184
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16093354","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Symmetric dimethylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"21917714","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processed","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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