8u1l

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

Method: ELECTRON MICROSCOPY Dmax: 128.3 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Heat shock protein 83

OrganismNot specified

UniProt A0A7E5VSK5

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–722 Chain B; UniProt 1–722 Mutation:0 RAF proto-oncogene serine/threonine-protein kinase × 1 (P04049) Hsp90 co-chaperone Cdc37, N-terminally processed × 1 (Q16543) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were blotted for 4.5 seconds before plunging Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A7E5VSK5_TRINI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–722; UniProt 1–722 Author chain B; PDBConstruct 1–722; UniProt 1–722

RAF proto-oncogene serine/threonine-protein kinase

Homo sapiens

UniProt P04049

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 2–648 Not recorded Heat shock protein 83 × 2 (A0A7E5VSK5) Hsp90 co-chaperone Cdc37, N-terminally processed × 1 (Q16543) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were blotted for 4.5 seconds before plunging Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

74 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAF1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 3–649; UniProt 2–648

Hsp90 co-chaperone Cdc37, N-terminally processed

Homo sapiens

UniProt Q16543

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–378 Mutation:0 Non-standard monomer:Yes (specific site not provided by mmCIF) Heat shock protein 83 × 2 (A0A7E5VSK5) RAF proto-oncogene serine/threonine-protein kinase × 1 (P04049) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE;Grids were blotted for 4.5 seconds before plunging Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDC37_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–378; UniProt 1–378

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8u1l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u1l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u1l
Deposition date deposition_date2023-09-01
Structure title titleCryo-EM structure of the RAF1-HSP90-CDC37 complex in the closed state
Keywords keywordsCRAF, RAF1, HSP90, CDC37, SIGNALING PROTEIN-CHAPERONE complex; SIGNALING PROTEIN/CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier39.48
Radius of gyration Rg (electron density) rg_electron38.90
Forward intensity I(0) i0482863000.00
Molecular weight molecular_weight179330.0 kDa
Excluded volume excluded_volume224710 ų
Envelope volume envelope_volume301730 ų
Hydration-shell volume shell_volume64034 ų
Envelope diameter envelope_diameter132.0
Shell Rg shell_rg45.08
Envelope Rg envelope_rg38.61
Shape Rg shape_rg38.87
Total Rg total_rg39.35
Total atoms total_atoms12595
Residues n_residues1542
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax128.3
Rg (real space) rg_real39.40
Rg uncertainty (real space) rg_real_error1.09
I(0) (real space) i0_real4.8290e+08
I(0) uncertainty (real space) i0_real_error7.5770e+06
Rg (reciprocal space) rg_reciprocal39.45
I(0) (reciprocal space) i0_reciprocal482900000.0000
Solution quality estimate total_estimate0.8887
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.1
Skewness Skewness skewness0.296
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha76570000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.890; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)