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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8GFT

Hsp90 provides platform for CRaf dephosphorylation by PP5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
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
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
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
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
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
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
C0000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006457biological_processprotein folding
C0006605biological_processprotein targeting
C0010608biological_processpost-transcriptional regulation of gene expression
C0019887molecular_functionprotein kinase regulator activity
C0019900molecular_functionkinase binding
C0019901molecular_functionprotein kinase binding
C0031072molecular_functionheat shock protein binding
C0050821biological_processprotein stabilization
C0051082molecular_functionunfolded protein binding
C0051087molecular_functionprotein-folding chaperone binding
C0051879molecular_functionHsp90 protein binding
C0060334biological_processregulation of type II interferon-mediated signaling pathway
C0060338biological_processregulation of type I interferon-mediated signaling pathway
C0070062cellular_componentextracellular exosome
C0097110molecular_functionscaffold protein binding
C0101031cellular_componentprotein folding chaperone complex
C1905091biological_processpositive regulation of type 2 mitophagy
C1990565cellular_componentHSP90-CDC37 chaperone complex
D0004672molecular_functionprotein kinase activity
D0005524molecular_functionATP binding
D0006468biological_processprotein phosphorylation
E0000165biological_processMAPK cascade
E0000278biological_processmitotic cell cycle
E0001965molecular_functionG-protein alpha-subunit binding
E0003723molecular_functionRNA binding
E0004721molecular_functionphosphoprotein phosphatase activity
E0004722molecular_functionprotein serine/threonine phosphatase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005886cellular_componentplasma membrane
E0006281biological_processDNA repair
E0006302biological_processdouble-strand break repair
E0006351biological_processDNA-templated transcription
E0006974biological_processDNA damage response
E0008017molecular_functionmicrotubule binding
E0008289molecular_functionlipid binding
E0010288biological_processresponse to lead ion
E0016787molecular_functionhydrolase activity
E0016791molecular_functionphosphatase activity
E0030291molecular_functionprotein serine/threonine kinase inhibitor activity
E0030544molecular_functionHsp70 protein binding
E0031072molecular_functionheat shock protein binding
E0031435molecular_functionmitogen-activated protein kinase kinase kinase binding
E0032991cellular_componentprotein-containing complex
E0042802molecular_functionidentical protein binding
E0043025cellular_componentneuronal cell body
E0043066biological_processnegative regulation of apoptotic process
E0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
E0043204cellular_componentperikaryon
E0043409biological_processnegative regulation of MAPK cascade
E0043531molecular_functionADP binding
E0044877molecular_functionprotein-containing complex binding
E0046872molecular_functionmetal ion binding
E0048156molecular_functiontau protein binding
E0051879molecular_functionHsp90 protein binding
E0070262biological_processpeptidyl-serine dephosphorylation
E0070301biological_processcellular response to hydrogen peroxide
E0071276biological_processcellular response to cadmium ion
E0101031cellular_componentprotein folding chaperone complex
E1904550biological_processresponse to arachidonate
E1990635cellular_componentproximal dendrite
E2000324biological_processpositive regulation of nuclear receptor-mediated glucocorticoid signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues21
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK
ChainResidueDetails
DILE355-LYS375
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKsnNIFL
ChainResidueDetails
DILE464-LEU476
site_idPS00298
Number of Residues10
DetailsHSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE
ChainResidueDetails
ATYR33-GLU42
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 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_FI6
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_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"PubMed","id":"23585225","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-methylated lysine","evidences":[{"source":"PubMed","id":"24880080","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"19696785","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11499","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues22
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI21
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_FI22
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_FI23
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16093354","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"Symmetric dimethylarginine; by PRMT5","evidences":[{"source":"PubMed","id":"21917714","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues33
DetailsRepeat: {"description":"TPR 1"}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues33
DetailsRepeat: {"description":"TPR 2"}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues33
DetailsRepeat: {"description":"TPR 3"}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15577939","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19601647","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1WAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H60","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H61","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H62","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H64","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15155720","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 472
ChainResidueDetails
EASP242metal ligand
EHIS427activator, metal ligand
EHIS244metal ligand
EASP271metal ligand
EASP274activator, proton donor
EARG275transition state stabiliser
EASN303metal ligand, transition state stabiliser
EALA304proton acceptor, proton donor, proton relay
EHIS352metal ligand
EARG400transition state stabiliser

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PDB entries from 2025-12-24

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