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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7Z38

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001890biological_processplacenta development
A0003723molecular_functionRNA binding
A0003725molecular_functiondouble-stranded RNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
A0006986biological_processresponse to unfolded protein
A0007004biological_processtelomere maintenance via telomerase
A0008180cellular_componentCOP9 signalosome
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0019062biological_processvirion attachment to host cell
A0019887molecular_functionprotein kinase regulator activity
A0019900molecular_functionkinase binding
A0019901molecular_functionprotein kinase binding
A0023026molecular_functionMHC class II protein complex binding
A0030235molecular_functionnitric-oxide synthase regulator activity
A0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
A0030911molecular_functionTPR domain binding
A0031072molecular_functionheat shock protein binding
A0031396biological_processregulation of protein ubiquitination
A0031625molecular_functionubiquitin protein ligase binding
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032880biological_processregulation of protein localization
A0032991cellular_componentprotein-containing complex
A0034605biological_processcellular response to heat
A0034751cellular_componentaryl hydrocarbon receptor complex
A0034774cellular_componentsecretory granule lumen
A0042277molecular_functionpeptide binding
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0042826molecular_functionhistone deacetylase binding
A0043008molecular_functionATP-dependent protein binding
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0044183molecular_functionprotein folding chaperone
A0044294cellular_componentdendritic growth cone
A0044295cellular_componentaxonal growth cone
A0045296molecular_functioncadherin binding
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0045597biological_processpositive regulation of cell differentiation
A0046983molecular_functionprotein dimerization activity
A0048156molecular_functiontau protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0050821biological_processprotein stabilization
A0051082molecular_functionunfolded protein binding
A0051131biological_processchaperone-mediated protein complex assembly
A0051726biological_processregulation of cell cycle
A0070062cellular_componentextracellular exosome
A0070182molecular_functionDNA polymerase binding
A0071353biological_processcellular response to interleukin-4
A0072542molecular_functionprotein phosphatase activator activity
A0097435biological_processsupramolecular fiber organization
A0097718molecular_functiondisordered domain specific binding
A0101031cellular_componentprotein folding chaperone complex
A0120293cellular_componentdynein axonemal particle
A0140662molecular_functionATP-dependent protein folding chaperone
A0141069molecular_functionreceptor ligand inhibitor activity
A1901799biological_processnegative regulation of proteasomal protein catabolic process
A1904813cellular_componentficolin-1-rich granule lumen
A1905323biological_processtelomerase holoenzyme complex assembly
A1990226molecular_functionhistone methyltransferase binding
A1990565cellular_componentHSP90-CDC37 chaperone complex
A2000010biological_processpositive regulation of protein localization to cell surface
B0000166molecular_functionnucleotide binding
B0001890biological_processplacenta development
B0003723molecular_functionRNA binding
B0003725molecular_functiondouble-stranded RNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
B0006986biological_processresponse to unfolded protein
B0007004biological_processtelomere maintenance via telomerase
B0008180cellular_componentCOP9 signalosome
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016887molecular_functionATP hydrolysis activity
B0019062biological_processvirion attachment to host cell
B0019887molecular_functionprotein kinase regulator activity
B0019900molecular_functionkinase binding
B0019901molecular_functionprotein kinase binding
B0023026molecular_functionMHC class II protein complex binding
B0030235molecular_functionnitric-oxide synthase regulator activity
B0030511biological_processpositive regulation of transforming growth factor beta receptor signaling pathway
B0030911molecular_functionTPR domain binding
B0031072molecular_functionheat shock protein binding
B0031396biological_processregulation of protein ubiquitination
B0031625molecular_functionubiquitin protein ligase binding
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032880biological_processregulation of protein localization
B0032991cellular_componentprotein-containing complex
B0034605biological_processcellular response to heat
B0034751cellular_componentaryl hydrocarbon receptor complex
B0034774cellular_componentsecretory granule lumen
B0042277molecular_functionpeptide binding
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0042826molecular_functionhistone deacetylase binding
B0043008molecular_functionATP-dependent protein binding
B0043025cellular_componentneuronal cell body
B0043066biological_processnegative regulation of apoptotic process
B0044183molecular_functionprotein folding chaperone
B0044294cellular_componentdendritic growth cone
B0044295cellular_componentaxonal growth cone
B0045296molecular_functioncadherin binding
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0045597biological_processpositive regulation of cell differentiation
B0046983molecular_functionprotein dimerization activity
B0048156molecular_functiontau protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0050821biological_processprotein stabilization
B0051082molecular_functionunfolded protein binding
B0051131biological_processchaperone-mediated protein complex assembly
B0051726biological_processregulation of cell cycle
B0070062cellular_componentextracellular exosome
B0070182molecular_functionDNA polymerase binding
B0071353biological_processcellular response to interleukin-4
B0072542molecular_functionprotein phosphatase activator activity
B0097435biological_processsupramolecular fiber organization
B0097718molecular_functiondisordered domain specific binding
B0101031cellular_componentprotein folding chaperone complex
B0120293cellular_componentdynein axonemal particle
B0140662molecular_functionATP-dependent protein folding chaperone
B0141069molecular_functionreceptor ligand inhibitor activity
B1901799biological_processnegative regulation of proteasomal protein catabolic process
B1904813cellular_componentficolin-1-rich granule lumen
B1905323biological_processtelomerase holoenzyme complex assembly
B1990226molecular_functionhistone methyltransferase binding
B1990565cellular_componentHSP90-CDC37 chaperone complex
B2000010biological_processpositive regulation of protein localization to cell surface
C0000165biological_processMAPK cascade
C0000166molecular_functionnucleotide binding
C0001678biological_processintracellular glucose homeostasis
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
C0008270molecular_functionzinc ion binding
C0008285biological_processnegative regulation of cell population proliferation
C0008286biological_processinsulin receptor signaling pathway
C0008625biological_processextrinsic apoptotic signaling pathway via death domain receptors
C0010856molecular_functionadenylate cyclase activator activity
C0014044biological_processSchwann cell development
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0019899molecular_functionenzyme binding
C0030154biological_processcell differentiation
C0030878biological_processthyroid gland development
C0031143cellular_componentpseudopodium
C0031267molecular_functionsmall GTPase binding
C0031333biological_processnegative regulation of protein-containing complex assembly
C0033138biological_processpositive regulation of peptidyl-serine phosphorylation
C0035019biological_processsomatic stem cell population maintenance
C0035023biological_processregulation of Rho protein signal transduction
C0035773biological_processinsulin secretion involved in cellular response to glucose stimulus
C0035994biological_processresponse to muscle stretch
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
C0044342biological_processtype B pancreatic cell proliferation
C0045104biological_processintermediate filament cytoskeleton organization
C0045595biological_processregulation of cell differentiation
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0046872molecular_functionmetal ion binding
C0048009biological_processinsulin-like growth factor receptor signaling pathway
C0048011biological_processneurotrophin TRK receptor signaling pathway
C0048538biological_processthymus development
C0060324biological_processface development
C0060333biological_processtype II interferon-mediated signaling pathway
C0071550biological_processdeath-inducing signaling complex assembly
C0106310molecular_functionprotein serine kinase activity
C1902042biological_processnegative regulation of extrinsic apoptotic signaling pathway via death domain receptors
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_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

238582

PDB entries from 2025-07-09

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