8U1L
Cryo-EM structure of the RAF1-HSP90-CDC37 complex in the closed state
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006457 | biological_process | protein folding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0051082 | molecular_function | unfolded protein binding |
A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006457 | biological_process | protein folding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0051082 | molecular_function | unfolded protein binding |
B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
C | 0000165 | biological_process | MAPK cascade |
C | 0001678 | biological_process | intracellular glucose homeostasis |
C | 0001934 | biological_process | positive regulation of protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0004709 | molecular_function | MAP kinase kinase kinase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005634 | cellular_component | nucleus |
C | 0005737 | cellular_component | cytoplasm |
C | 0005739 | cellular_component | mitochondrion |
C | 0005741 | cellular_component | mitochondrial outer membrane |
C | 0005794 | cellular_component | Golgi apparatus |
C | 0005829 | cellular_component | cytosol |
C | 0005886 | cellular_component | plasma membrane |
C | 0006468 | biological_process | protein phosphorylation |
C | 0006915 | biological_process | apoptotic process |
C | 0007165 | biological_process | signal transduction |
C | 0007190 | biological_process | activation of adenylate cyclase activity |
C | 0008285 | biological_process | negative regulation of cell population proliferation |
C | 0008286 | biological_process | insulin receptor signaling pathway |
C | 0008625 | biological_process | extrinsic apoptotic signaling pathway via death domain receptors |
C | 0014044 | biological_process | Schwann cell development |
C | 0019899 | molecular_function | enzyme binding |
C | 0030154 | biological_process | cell differentiation |
C | 0030878 | biological_process | thyroid gland development |
C | 0031143 | cellular_component | pseudopodium |
C | 0031267 | molecular_function | small GTPase binding |
C | 0031333 | biological_process | negative regulation of protein-containing complex assembly |
C | 0033138 | biological_process | positive regulation of peptidyl-serine phosphorylation |
C | 0035019 | biological_process | somatic stem cell population maintenance |
C | 0035023 | biological_process | regulation of Rho protein signal transduction |
C | 0035773 | biological_process | insulin secretion involved in cellular response to glucose stimulus |
C | 0035994 | biological_process | response to muscle stretch |
C | 0036211 | biological_process | protein modification process |
C | 0038133 | biological_process | ERBB2-ERBB3 signaling pathway |
C | 0042060 | biological_process | wound healing |
C | 0042552 | biological_process | myelination |
C | 0042802 | molecular_function | identical protein binding |
C | 0042981 | biological_process | regulation of apoptotic process |
C | 0043066 | biological_process | negative regulation of apoptotic process |
C | 0043154 | biological_process | negative regulation of cysteine-type endopeptidase activity involved in apoptotic process |
C | 0043410 | biological_process | positive regulation of MAPK cascade |
C | 0044342 | biological_process | type B pancreatic cell proliferation |
C | 0045104 | biological_process | intermediate filament cytoskeleton organization |
C | 0045595 | biological_process | regulation of cell differentiation |
C | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
C | 0046872 | molecular_function | metal ion binding |
C | 0048009 | biological_process | insulin-like growth factor receptor signaling pathway |
C | 0048011 | biological_process | neurotrophin TRK receptor signaling pathway |
C | 0048538 | biological_process | thymus development |
C | 0060324 | biological_process | face development |
C | 0060333 | biological_process | type II interferon-mediated signaling pathway |
C | 0071550 | biological_process | death-inducing signaling complex assembly |
C | 0106310 | molecular_function | protein serine kinase activity |
C | 1902042 | biological_process | negative regulation of extrinsic apoptotic signaling pathway via death domain receptors |
C | 1902531 | biological_process | regulation of intracellular signal transduction |
C | 2000145 | biological_process | regulation of cell motility |
D | 0000079 | biological_process | regulation of cyclin-dependent protein serine/threonine kinase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006457 | biological_process | protein folding |
D | 0006605 | biological_process | protein targeting |
D | 0010608 | biological_process | post-transcriptional regulation of gene expression |
D | 0019887 | molecular_function | protein kinase regulator activity |
D | 0019900 | molecular_function | kinase binding |
D | 0019901 | molecular_function | protein kinase binding |
D | 0031072 | molecular_function | heat shock protein binding |
D | 0050821 | biological_process | protein stabilization |
D | 0051082 | molecular_function | unfolded protein binding |
D | 0051087 | molecular_function | protein-folding chaperone binding |
D | 0051879 | molecular_function | Hsp90 protein binding |
D | 0060334 | biological_process | regulation of type II interferon-mediated signaling pathway |
D | 0060338 | biological_process | regulation of type I interferon-mediated signaling pathway |
D | 0070062 | cellular_component | extracellular exosome |
D | 0097110 | molecular_function | scaffold protein binding |
D | 0098779 | biological_process | positive regulation of mitophagy in response to mitochondrial depolarization |
D | 0101031 | cellular_component | protein folding chaperone complex |
D | 1990565 | cellular_component | HSP90-CDC37 chaperone complex |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 21 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGSFGTVYkGkwhgd.............VAVK |
Chain | Residue | Details |
C | ILE355-LYS375 |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDMKsnNIFL |
Chain | Residue | Details |
C | ILE464-LEU476 |
site_id | PS00298 |
Number of Residues | 10 |
Details | HSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE |
Chain | Residue | Details |
A | TYR33-GLU42 |
site_id | PS00479 |
Number of Residues | 46 |
Details | ZF_DAG_PE_1 Zinc finger phorbol-ester/DAG-type signature. HnFarktflklaf.CdiCqkfLlngfr.....CqtCgykfHehCstkvptm..C |
Chain | Residue | Details |
C | HIS139-CYS184 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
D | MET1 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-terminally processed => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
D | VAL2 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692 |
Chain | Residue | Details |
D | SEP13 | |
C | CYS152 | |
C | CYS155 | |
C | CYS165 | |
C | CYS168 | |
C | HIS173 | |
C | CYS176 | |
C | CYS184 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
D | LYS78 | |
D | LYS154 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | THR118 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | SER120 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
D | SER377 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_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 |
Chain | Residue | Details |
C | SER259 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:8349614 |
Chain | Residue | Details |
C | THR268 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by PKA => ECO:0000269|PubMed:7477354 |
Chain | Residue | Details |
C | THR269 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by MAPK1 => ECO:0000269|PubMed:21917714, ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
C | SER289 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER296 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by MAPK1 => ECO:0000269|PubMed:21917714, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER301 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_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 |
Chain | Residue | Details |
C | SER338 |
site_id | SWS_FT_FI15 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PAK1, PAK2 and PAK3 => ECO:0000269|PubMed:15849194 |
Chain | Residue | Details |
C | SER339 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:16892053 |
Chain | Residue | Details |
C | TYR340 | |
C | TYR341 |
site_id | SWS_FT_FI17 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:16093354 |
Chain | Residue | Details |
C | SER471 |
site_id | SWS_FT_FI18 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:11447113 |
Chain | Residue | Details |
C | THR491 |
site_id | SWS_FT_FI19 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11447113 |
Chain | Residue | Details |
C | SER494 |
site_id | SWS_FT_FI20 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKC => ECO:0000269|PubMed:8349614 |
Chain | Residue | Details |
C | SER499 |
site_id | SWS_FT_FI21 |
Number of Residues | 1 |
Details | MOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:21917714 |
Chain | Residue | Details |
C | ARG563 |
site_id | SWS_FT_FI22 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:10801873, ECO:0000269|PubMed:16892053, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:8349614 |
Chain | Residue | Details |
C | SER621 |
site_id | SWS_FT_FI23 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by MAPK1 => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER642 |