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8H77

Hsp90-AhR-p23-XAP2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001890biological_processplacenta development
A0002134molecular_functionUTP binding
A0002135molecular_functionCTP binding
A0003725molecular_functiondouble-stranded RNA binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005765cellular_componentlysosomal membrane
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006457biological_processprotein folding
A0007004biological_processtelomere maintenance via telomerase
A0008180cellular_componentCOP9 signalosome
A0009986cellular_componentcell surface
A0016234cellular_componentinclusion body
A0016323cellular_componentbasolateral plasma membrane
A0016324cellular_componentapical plasma membrane
A0016887molecular_functionATP hydrolysis activity
A0017098molecular_functionsulfonylurea receptor binding
A0019062biological_processvirion attachment to host cell
A0019887molecular_functionprotein kinase regulator activity
A0019900molecular_functionkinase binding
A0019901molecular_functionprotein kinase 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
A0031526cellular_componentbrush border membrane
A0031625molecular_functionubiquitin protein ligase binding
A0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
A0032564molecular_functiondATP binding
A0032880biological_processregulation of protein localization
A0032991cellular_componentprotein-containing complex
A0034605biological_processcellular response to heat
A0034751cellular_componentaryl hydrocarbon receptor complex
A0042277molecular_functionpeptide binding
A0042307biological_processpositive regulation of protein import into nucleus
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
A0043524biological_processnegative regulation of neuron apoptotic process
A0044183molecular_functionprotein folding chaperone
A0044294cellular_componentdendritic growth cone
A0044295cellular_componentaxonal growth cone
A0044325molecular_functiontransmembrane transporter binding
A0045429biological_processpositive regulation of nitric oxide biosynthetic process
A0045597biological_processpositive regulation of cell differentiation
A0045793biological_processpositive regulation of cell size
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
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
A1901363molecular_functionheterocyclic compound binding
A1901799biological_processnegative regulation of proteasomal protein catabolic process
A1903660biological_processnegative regulation of complement-dependent cytotoxicity
A1905323biological_processtelomerase holoenzyme complex assembly
A1990226molecular_functionhistone methyltransferase binding
A1990565cellular_componentHSP90-CDC37 chaperone complex
A1990913cellular_componentsperm head plasma membrane
A1990917cellular_componentooplasm
A2000010biological_processpositive regulation of protein localization to cell surface
B0000166molecular_functionnucleotide binding
B0001890biological_processplacenta development
B0002134molecular_functionUTP binding
B0002135molecular_functionCTP binding
B0003725molecular_functiondouble-stranded RNA binding
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005525molecular_functionGTP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006457biological_processprotein folding
B0007004biological_processtelomere maintenance via telomerase
B0008180cellular_componentCOP9 signalosome
B0009986cellular_componentcell surface
B0016234cellular_componentinclusion body
B0016323cellular_componentbasolateral plasma membrane
B0016324cellular_componentapical plasma membrane
B0016887molecular_functionATP hydrolysis activity
B0017098molecular_functionsulfonylurea receptor binding
B0019062biological_processvirion attachment to host cell
B0019887molecular_functionprotein kinase regulator activity
B0019900molecular_functionkinase binding
B0019901molecular_functionprotein kinase 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
B0031526cellular_componentbrush border membrane
B0031625molecular_functionubiquitin protein ligase binding
B0032435biological_processnegative regulation of proteasomal ubiquitin-dependent protein catabolic process
B0032564molecular_functiondATP binding
B0032880biological_processregulation of protein localization
B0032991cellular_componentprotein-containing complex
B0034605biological_processcellular response to heat
B0034751cellular_componentaryl hydrocarbon receptor complex
B0042277molecular_functionpeptide binding
B0042307biological_processpositive regulation of protein import into nucleus
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
B0043524biological_processnegative regulation of neuron apoptotic process
B0044183molecular_functionprotein folding chaperone
B0044294cellular_componentdendritic growth cone
B0044295cellular_componentaxonal growth cone
B0044325molecular_functiontransmembrane transporter binding
B0045429biological_processpositive regulation of nitric oxide biosynthetic process
B0045597biological_processpositive regulation of cell differentiation
B0045793biological_processpositive regulation of cell size
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
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
B1901363molecular_functionheterocyclic compound binding
B1901799biological_processnegative regulation of proteasomal protein catabolic process
B1903660biological_processnegative regulation of complement-dependent cytotoxicity
B1905323biological_processtelomerase holoenzyme complex assembly
B1990226molecular_functionhistone methyltransferase binding
B1990565cellular_componentHSP90-CDC37 chaperone complex
B1990913cellular_componentsperm head plasma membrane
B1990917cellular_componentooplasm
B2000010biological_processpositive regulation of protein localization to cell surface
C0001516biological_processprostaglandin biosynthetic process
C0002039molecular_functionp53 binding
C0003720molecular_functiontelomerase activity
C0005634cellular_componentnucleus
C0005697cellular_componenttelomerase holoenzyme complex
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005884cellular_componentactin filament
C0005978biological_processglycogen biosynthetic process
C0006457biological_processprotein folding
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0006693biological_processprostaglandin metabolic process
C0007004biological_processtelomere maintenance via telomerase
C0008283biological_processcell population proliferation
C0010628biological_processpositive regulation of gene expression
C0016853molecular_functionisomerase activity
C0019371biological_processcyclooxygenase pathway
C0019899molecular_functionenzyme binding
C0032212biological_processpositive regulation of telomere maintenance via telomerase
C0032991cellular_componentprotein-containing complex
C0042921biological_processnuclear receptor-mediated glucocorticoid signaling pathway
C0043025cellular_componentneuronal cell body
C0043588biological_processskin development
C0048471cellular_componentperinuclear region of cytoplasm
C0050220molecular_functionprostaglandin-E synthase activity
C0050821biological_processprotein stabilization
C0051082molecular_functionunfolded protein binding
C0051087molecular_functionprotein-folding chaperone binding
C0051131biological_processchaperone-mediated protein complex assembly
C0051402biological_processneuron apoptotic process
C0051879molecular_functionHsp90 protein binding
C0060430biological_processlung saccule development
C0070182molecular_functionDNA polymerase binding
C0101031cellular_componentprotein folding chaperone complex
C1905323biological_processtelomerase holoenzyme complex assembly
D0001516biological_processprostaglandin biosynthetic process
D0002039molecular_functionp53 binding
D0003720molecular_functiontelomerase activity
D0005634cellular_componentnucleus
D0005697cellular_componenttelomerase holoenzyme complex
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005884cellular_componentactin filament
D0005978biological_processglycogen biosynthetic process
D0006457biological_processprotein folding
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0006693biological_processprostaglandin metabolic process
D0007004biological_processtelomere maintenance via telomerase
D0008283biological_processcell population proliferation
D0010628biological_processpositive regulation of gene expression
D0016853molecular_functionisomerase activity
D0019371biological_processcyclooxygenase pathway
D0019899molecular_functionenzyme binding
D0032212biological_processpositive regulation of telomere maintenance via telomerase
D0032991cellular_componentprotein-containing complex
D0042921biological_processnuclear receptor-mediated glucocorticoid signaling pathway
D0043025cellular_componentneuronal cell body
D0043588biological_processskin development
D0048471cellular_componentperinuclear region of cytoplasm
D0050220molecular_functionprostaglandin-E synthase activity
D0050821biological_processprotein stabilization
D0051082molecular_functionunfolded protein binding
D0051087molecular_functionprotein-folding chaperone binding
D0051131biological_processchaperone-mediated protein complex assembly
D0051402biological_processneuron apoptotic process
D0051879molecular_functionHsp90 protein binding
D0060430biological_processlung saccule development
D0070182molecular_functionDNA polymerase binding
D0101031cellular_componentprotein folding chaperone complex
D1905323biological_processtelomerase holoenzyme complex assembly
E0006355biological_processregulation of DNA-templated transcription
E0006805biological_processxenobiotic metabolic process
E0009410biological_processresponse to xenobiotic stimulus
E0046983molecular_functionprotein dimerization activity
F0003712molecular_functiontranscription coregulator activity
F0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0005886cellular_componentplasma membrane
F0006626biological_processprotein targeting to mitochondrion
F0006805biological_processxenobiotic metabolic process
F0010737biological_processprotein kinase A signaling
F0016020cellular_componentmembrane
F0017162molecular_functionaryl hydrocarbon receptor binding
F0019899molecular_functionenzyme binding
F0034751cellular_componentaryl hydrocarbon receptor complex
F0036004molecular_functionGAF domain binding
F0051082molecular_functionunfolded protein binding
F0051604biological_processprotein maturation
Functional Information from PROSITE/UniProt
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 Residues10
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Cleaved under oxidative stress","evidences":[{"source":"UniProtKB","id":"P08238","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P08238","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P08238","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P08238","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P08238","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"17947660","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-methylated lysine","evidences":[{"source":"UniProtKB","id":"P08238","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P08238","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"22556278","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues178
DetailsDomain: {"description":"CS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00547","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q15185","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15378723","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15345747","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18630941","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19144319","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"Q15185","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues67
DetailsDomain: {"description":"PAS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00140","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues38
DetailsDomain: {"description":"PAC"}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues33
DetailsRepeat: {"description":"TPR 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues33
DetailsRepeat: {"description":"TPR 2","evidences":[{"source":"UniProtKB","id":"O00170","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues33
DetailsRepeat: {"description":"TPR 3","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O00170","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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