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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7Z37

Structure of the RAF1-HSP90-CDC37 complex (RHC-II)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AP10000166molecular_functionnucleotide binding
AP10003723molecular_functionRNA binding
AP10003725molecular_functiondouble-stranded RNA binding
AP10005515molecular_functionprotein binding
AP10005524molecular_functionATP binding
AP10005576cellular_componentextracellular region
AP10005634cellular_componentnucleus
AP10005654cellular_componentnucleoplasm
AP10005737cellular_componentcytoplasm
AP10005739cellular_componentmitochondrion
AP10005829cellular_componentcytosol
AP10005886cellular_componentplasma membrane
AP10006457biological_processprotein folding
AP10006986biological_processresponse to unfolded protein
AP10007004biological_processtelomere maintenance via telomerase
AP10008180cellular_componentCOP9 signalosome
AP10009986cellular_componentcell surface
AP10016020cellular_componentmembrane
AP10016887molecular_functionATP hydrolysis activity
AP10019062biological_processvirion attachment to host cell
AP10019887molecular_functionprotein kinase regulator activity
AP10019900molecular_functionkinase binding
AP10019901molecular_functionprotein kinase binding
AP10023026molecular_functionMHC class II protein complex binding
AP10030235molecular_functionnitric-oxide synthase regulator activity
AP10030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
AP10030911molecular_functionTPR domain binding
AP10031072molecular_functionheat shock protein binding
AP10031396biological_processregulation of protein ubiquitination
AP10031625molecular_functionubiquitin protein ligase binding
AP10032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
AP10032880biological_processregulation of protein localization
AP10032991cellular_componentprotein-containing complex
AP10034605biological_processcellular response to heat
AP10034751cellular_componentaryl hydrocarbon receptor complex
AP10034774cellular_componentsecretory granule lumen
AP10042277molecular_functionpeptide binding
AP10042470cellular_componentmelanosome
AP10042802molecular_functionidentical protein binding
AP10042803molecular_functionprotein homodimerization activity
AP10042826molecular_functionhistone deacetylase binding
AP10043008molecular_functionATP-dependent protein binding
AP10043025cellular_componentneuronal cell body
AP10044183molecular_functionprotein folding chaperone
AP10044294cellular_componentdendritic growth cone
AP10044295cellular_componentaxonal growth cone
AP10045296molecular_functioncadherin binding
AP10045429biological_processpositive regulation of nitric oxide biosynthetic process
AP10045597biological_processpositive regulation of cell differentiation
AP10046983molecular_functionprotein dimerization activity
AP10048156molecular_functiontau protein binding
AP10048471cellular_componentperinuclear region of cytoplasm
AP10050821biological_processprotein stabilization
AP10051082molecular_functionunfolded protein binding
AP10051131biological_processchaperone-mediated protein complex assembly
AP10051726biological_processregulation of cell cycle
AP10070062cellular_componentextracellular exosome
AP10070182molecular_functionDNA polymerase binding
AP10072542molecular_functionprotein phosphatase activator activity
AP10097435biological_processsupramolecular fiber organization
AP10097718molecular_functiondisordered domain specific binding
AP10101031cellular_componentprotein folding chaperone complex
AP10120293cellular_componentdynein axonemal particle
AP10140662molecular_functionATP-dependent protein folding chaperone
AP10141069molecular_functionreceptor ligand inhibitor activity
AP11901799biological_processnegative regulation of proteasomal protein catabolic process
AP11904813cellular_componentficolin-1-rich granule lumen
AP11905323biological_processtelomerase holoenzyme complex assembly
AP11990226molecular_functionhistone methyltransferase binding
AP11990565cellular_componentHSP90-CDC37 chaperone complex
AP12000010biological_processpositive regulation of protein localization to cell surface
BP10000166molecular_functionnucleotide binding
BP10003723molecular_functionRNA binding
BP10003725molecular_functiondouble-stranded RNA binding
BP10005515molecular_functionprotein binding
BP10005524molecular_functionATP binding
BP10005576cellular_componentextracellular region
BP10005634cellular_componentnucleus
BP10005654cellular_componentnucleoplasm
BP10005737cellular_componentcytoplasm
BP10005739cellular_componentmitochondrion
BP10005829cellular_componentcytosol
BP10005886cellular_componentplasma membrane
BP10006457biological_processprotein folding
BP10006986biological_processresponse to unfolded protein
BP10007004biological_processtelomere maintenance via telomerase
BP10008180cellular_componentCOP9 signalosome
BP10009986cellular_componentcell surface
BP10016020cellular_componentmembrane
BP10016887molecular_functionATP hydrolysis activity
BP10019062biological_processvirion attachment to host cell
BP10019887molecular_functionprotein kinase regulator activity
BP10019900molecular_functionkinase binding
BP10019901molecular_functionprotein kinase binding
BP10023026molecular_functionMHC class II protein complex binding
BP10030235molecular_functionnitric-oxide synthase regulator activity
BP10030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
BP10030911molecular_functionTPR domain binding
BP10031072molecular_functionheat shock protein binding
BP10031396biological_processregulation of protein ubiquitination
BP10031625molecular_functionubiquitin protein ligase binding
BP10032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
BP10032880biological_processregulation of protein localization
BP10032991cellular_componentprotein-containing complex
BP10034605biological_processcellular response to heat
BP10034751cellular_componentaryl hydrocarbon receptor complex
BP10034774cellular_componentsecretory granule lumen
BP10042277molecular_functionpeptide binding
BP10042470cellular_componentmelanosome
BP10042802molecular_functionidentical protein binding
BP10042803molecular_functionprotein homodimerization activity
BP10042826molecular_functionhistone deacetylase binding
BP10043008molecular_functionATP-dependent protein binding
BP10043025cellular_componentneuronal cell body
BP10044183molecular_functionprotein folding chaperone
BP10044294cellular_componentdendritic growth cone
BP10044295cellular_componentaxonal growth cone
BP10045296molecular_functioncadherin binding
BP10045429biological_processpositive regulation of nitric oxide biosynthetic process
BP10045597biological_processpositive regulation of cell differentiation
BP10046983molecular_functionprotein dimerization activity
BP10048156molecular_functiontau protein binding
BP10048471cellular_componentperinuclear region of cytoplasm
BP10050821biological_processprotein stabilization
BP10051082molecular_functionunfolded protein binding
BP10051131biological_processchaperone-mediated protein complex assembly
BP10051726biological_processregulation of cell cycle
BP10070062cellular_componentextracellular exosome
BP10070182molecular_functionDNA polymerase binding
BP10072542molecular_functionprotein phosphatase activator activity
BP10097435biological_processsupramolecular fiber organization
BP10097718molecular_functiondisordered domain specific binding
BP10101031cellular_componentprotein folding chaperone complex
BP10120293cellular_componentdynein axonemal particle
BP10140662molecular_functionATP-dependent protein folding chaperone
BP10141069molecular_functionreceptor ligand inhibitor activity
BP11901799biological_processnegative regulation of proteasomal protein catabolic process
BP11904813cellular_componentficolin-1-rich granule lumen
BP11905323biological_processtelomerase holoenzyme complex assembly
BP11990226molecular_functionhistone methyltransferase binding
BP11990565cellular_componentHSP90-CDC37 chaperone complex
BP12000010biological_processpositive regulation of protein localization to cell surface
CP10000165biological_processMAPK cascade
CP10000166molecular_functionnucleotide binding
CP10004672molecular_functionprotein kinase activity
CP10004674molecular_functionprotein serine/threonine kinase activity
CP10004709molecular_functionMAP kinase kinase kinase activity
CP10005515molecular_functionprotein binding
CP10005524molecular_functionATP binding
CP10005634cellular_componentnucleus
CP10005737cellular_componentcytoplasm
CP10005739cellular_componentmitochondrion
CP10005741cellular_componentmitochondrial outer membrane
CP10005794cellular_componentGolgi apparatus
CP10005829cellular_componentcytosol
CP10005886cellular_componentplasma membrane
CP10006468biological_processprotein phosphorylation
CP10006915biological_processapoptotic process
CP10007165biological_processsignal transduction
CP10007528biological_processneuromuscular junction development
CP10008270molecular_functionzinc ion binding
CP10008285biological_processnegative regulation of cell population proliferation
CP10008286biological_processinsulin receptor signaling pathway
CP10010856molecular_functionadenylate cyclase activator activity
CP10014044biological_processSchwann cell development
CP10016301molecular_functionkinase activity
CP10016740molecular_functiontransferase activity
CP10019899molecular_functionenzyme binding
CP10031143cellular_componentpseudopodium
CP10031267molecular_functionsmall GTPase binding
CP10031333biological_processnegative regulation of protein-containing complex assembly
CP10033138biological_processpositive regulation of peptidyl-serine phosphorylation
CP10035023biological_processregulation of Rho protein signal transduction
CP10038127biological_processERBB signaling pathway
CP10038133biological_processERBB2-ERBB3 signaling pathway
CP10042060biological_processwound healing
CP10042552biological_processmyelination
CP10042802molecular_functionidentical protein binding
CP10042981biological_processregulation of apoptotic process
CP10043066biological_processnegative regulation of apoptotic process
CP10043410biological_processpositive regulation of MAPK cascade
CP10045595biological_processregulation of cell differentiation
CP10046872molecular_functionmetal ion binding
CP10048009biological_processinsulin-like growth factor receptor signaling pathway
CP10060333biological_processtype II interferon-mediated signaling pathway
CP10106310molecular_functionprotein serine kinase activity
DP10000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
DP10005515molecular_functionprotein binding
DP10005737cellular_componentcytoplasm
DP10005829cellular_componentcytosol
DP10006457biological_processprotein folding
DP10006605biological_processprotein targeting
DP10010608biological_processpost-transcriptional regulation of gene expression
DP10019887molecular_functionprotein kinase regulator activity
DP10019900molecular_functionkinase binding
DP10019901molecular_functionprotein kinase binding
DP10031072molecular_functionheat shock protein binding
DP10050821biological_processprotein stabilization
DP10051082molecular_functionunfolded protein binding
DP10051087molecular_functionprotein-folding chaperone binding
DP10051879molecular_functionHsp90 protein binding
DP10060334biological_processregulation of type II interferon-mediated signaling pathway
DP10060338biological_processregulation of type I interferon-mediated signaling pathway
DP10070062cellular_componentextracellular exosome
DP10097110molecular_functionscaffold protein binding
DP10101031cellular_componentprotein folding chaperone complex
DP11905091biological_processpositive regulation of type 2 mitophagy
DP11990565cellular_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
CP1ILE355-LYS375
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKsnNIFL
ChainResidueDetails
CP1ILE464-LEU476
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
AP1TYR33-GLU42
site_idPS00479
Number of Residues46
DetailsZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HnFarktflklaf.CdiCqkfLlngfr.....CqtCgykfHehCstkvptm..C
ChainResidueDetails
CP1HIS139-CYS184
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Cleaved under oxidative stress","evidences":[{"source":"PubMed","id":"22848402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"23585225","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-methylated lysine","evidences":[{"source":"PubMed","id":"24880080","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"19696785","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18088087","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18318008","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16093354","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Symmetric dimethylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"21917714","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI24
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_FI25
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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