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8U1L

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0016887molecular_functionATP hydrolysis activity
A0051082molecular_functionunfolded protein binding
A0140662molecular_functionATP-dependent protein folding chaperone
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006457biological_processprotein folding
B0016887molecular_functionATP hydrolysis activity
B0051082molecular_functionunfolded protein binding
B0140662molecular_functionATP-dependent protein folding chaperone
C0000165biological_processMAPK cascade
C0001678biological_processintracellular glucose homeostasis
C0001934biological_processpositive regulation of protein phosphorylation
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
C0007190biological_processactivation of adenylate cyclase activity
C0008285biological_processnegative regulation of cell population proliferation
C0008286biological_processinsulin receptor signaling pathway
C0008625biological_processextrinsic apoptotic signaling pathway via death domain receptors
C0014044biological_processSchwann cell development
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
C0036211biological_processprotein modification process
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
C0043154biological_processnegative regulation of cysteine-type endopeptidase activity involved in 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
C1902531biological_processregulation of intracellular signal transduction
C2000145biological_processregulation of cell motility
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
D0098779biological_processpositive regulation of mitophagy in response to mitochondrial depolarization
D0101031cellular_componentprotein folding chaperone complex
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 Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330
ChainResidueDetails
DMET1

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processed => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
DVAL2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
DSEP13
CCYS152
CCYS155
CCYS165
CCYS168
CHIS173
CCYS176
CCYS184

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
DLYS78
DLYS154

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DTHR118

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER120

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
DSER377

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA, PKC and PKB/AKT1 => ECO:0000269|PubMed:10576742, ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:11756411, ECO:0000269|PubMed:15047712, ECO:0000269|PubMed:16630891, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:8349614
ChainResidueDetails
CSER259

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:8349614
ChainResidueDetails
CTHR268

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:7477354
ChainResidueDetails
CTHR269

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK1 => ECO:0000269|PubMed:21917714, ECO:0007744|PubMed:19690332
ChainResidueDetails
CSER289

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER296

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK1 => ECO:0000269|PubMed:21917714, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER301

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PAK1, PAK2, PAK3 and PAK5 => ECO:0000269|PubMed:11733498, ECO:0000269|PubMed:15849194, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:18465753, ECO:0000269|PubMed:21917714
ChainResidueDetails
CSER338

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PAK1, PAK2 and PAK3 => ECO:0000269|PubMed:15849194
ChainResidueDetails
CSER339

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:16892053
ChainResidueDetails
CTYR340
CTYR341

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16093354
ChainResidueDetails
CSER471

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:11447113
ChainResidueDetails
CTHR491

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:11447113
ChainResidueDetails
CSER494

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8349614
ChainResidueDetails
CSER499

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:21917714
ChainResidueDetails
CARG563

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:8349614
ChainResidueDetails
CSER621

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MAPK1 => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER642

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PDB entries from 2024-07-24

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