8gae

Hsp90 provides platform for CRaf dephosphorylation by PP5

Method: ELECTRON MICROSCOPY Dmax: 171.2 Å Quality: GOOD

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

Heat shock protein HSP 90-beta

Homo sapiens

UniProt P08238

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–724 Chain B; UniProt 1–724 Not recorded Hsp90 co-chaperone Cdc37 × 1 (Q16543) RAF proto-oncogene serine/threonine-protein kinase × 1 (P04049) Serine/threonine-protein phosphatase 5 × 1 (P53041) K POTASSIUM ION × 2 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3UL OF SAMPLE 10C 100% HUMIDITY 30S WAIT TIME 3S BLOT TIME -2 BLOT FORCE Resolution 3.30 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.

29 other PDB entries and 50 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HS90B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–727; UniProt 1–724 Author chain B; PDBConstruct 4–727; UniProt 1–724

Hsp90 co-chaperone Cdc37

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 1–378 Non-standard monomer:Yes (specific site not provided by mmCIF) Heat shock protein HSP 90-beta × 2 (P08238) RAF proto-oncogene serine/threonine-protein kinase × 1 (P04049) Serine/threonine-protein phosphatase 5 × 1 (P53041) K POTASSIUM ION × 2 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3UL OF SAMPLE 10C 100% HUMIDITY 30S WAIT TIME 3S BLOT TIME -2 BLOT FORCE Resolution 3.30 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 2
Chains and sequence ranges Author chain C; PDBConstruct 1–378; UniProt 1–378

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 404–610 Not recorded Heat shock protein HSP 90-beta × 2 (P08238) Hsp90 co-chaperone Cdc37 × 1 (Q16543) Serine/threonine-protein phosphatase 5 × 1 (P53041) K POTASSIUM ION × 2 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3UL OF SAMPLE 10C 100% HUMIDITY 30S WAIT TIME 3S BLOT TIME -2 BLOT FORCE Resolution 3.30 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 3
Chains and sequence ranges Author chain D; PDBConstruct 1–207; UniProt 404–610

Serine/threonine-protein phosphatase 5

Homo sapiens

UniProt P53041

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 1–499 Mutation:H304A Heat shock protein HSP 90-beta × 2 (P08238) Hsp90 co-chaperone Cdc37 × 1 (Q16543) RAF proto-oncogene serine/threonine-protein kinase × 1 (P04049) K POTASSIUM ION × 2 MG MAGNESIUM ION × 2 ADP ADENOSINE-5'-DIPHOSPHATE × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MN MANGANESE (II) ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;3UL OF SAMPLE 10C 100% HUMIDITY 30S WAIT TIME 3S BLOT TIME -2 BLOT FORCE Resolution 3.30 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.

21 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPP5_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 5–503; UniProt 1–499

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 8gae

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8gae
Deposition date deposition_date2023-02-22
Structure title titleHsp90 provides platform for CRaf dephosphorylation by PP5
Keywords keywordschaperone, kinase, phosphatase, complex; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.53
Radius of gyration Rg (electron density) rg_electron46.26
Forward intensity I(0) i0937180000.00
Molecular weight molecular_weight252750.0 kDa
Excluded volume excluded_volume316490 ų
Envelope volume envelope_volume459710 ų
Hydration-shell volume shell_volume83800 ų
Envelope diameter envelope_diameter180.8
Shell Rg shell_rg50.17
Envelope Rg envelope_rg46.01
Shape Rg shape_rg46.27
Total Rg total_rg46.40
Total atoms total_atoms35406
Residues n_residues2174
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 dmax171.2
Rg (real space) rg_real46.61
Rg uncertainty (real space) rg_real_error2.02
I(0) (real space) i0_real9.3720e+08
I(0) uncertainty (real space) i0_real_error1.7380e+07
Rg (reciprocal space) rg_reciprocal46.53
I(0) (reciprocal space) i0_reciprocal937100000.0000
Solution quality estimate total_estimate0.8286
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.4
Skewness Skewness skewness0.497
Kurtosis Kurtosis kurtosis0.178
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha87100000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.613; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.930

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8gaeD01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology510 — Transferase(Phosphotransferase); domain 1
Homologous superfamily homologous superfamily10 — Transferase(Phosphotransferase) domain 1
Domain ID domain_id8gaeE01
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily10 — Tetratricopeptide repeat domain
Domain ID domain_id8gaeE02
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology21 — Purple Acid Phosphatase; chain A, domain 2
Homologous superfamily homologous superfamily10 — Metallo-dependent phosphatases

8. Citations (1)

9. Files and Curves (10)