5fwm

Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex

Method: ELECTRON MICROSCOPY Dmax: 145.5 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–724 Chain B; UniProt 1–724 Not recorded HSP90 CO-CHAPERONE CDC37 × 1 (Q16543) CYCLIN-DEPENDENT KINASE 4 × 1 (P11802) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:20MM TRIS-HCL (PH 7.5), 150 MM NACL, 10 MM KCL, 10 MM MGCL2, 20 MM NA2MOO4, 2MM DTT, 0.085MM DDM;pH 7.5;20MM TRIS-HCL (PH 7.5), 150 MM NACL, 10 MM KCL, 10 MM MGCL2, 20 MM NA2MOO4, 2MM DTT, 0.085MM DDM cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 8.00 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–378 Non-standard monomer:Yes (specific site not provided by mmCIF) HEAT SHOCK PROTEIN HSP 90 BETA × 2 (P08238) CYCLIN-DEPENDENT KINASE 4 × 1 (P11802) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:20MM TRIS-HCL (PH 7.5), 150 MM NACL, 10 MM KCL, 10 MM MGCL2, 20 MM NA2MOO4, 2MM DTT, 0.085MM DDM;pH 7.5;20MM TRIS-HCL (PH 7.5), 150 MM NACL, 10 MM KCL, 10 MM MGCL2, 20 MM NA2MOO4, 2MM DTT, 0.085MM DDM cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 8.00 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 E; PDBConstruct 1–378; UniProt 1–378

CYCLIN-DEPENDENT KINASE 4

HOMO SAPIENS

UniProt P11802

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 K; UniProt 1–303 Not recorded HEAT SHOCK PROTEIN HSP 90 BETA × 2 (P08238) HSP90 CO-CHAPERONE CDC37 × 1 (Q16543) ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:20MM TRIS-HCL (PH 7.5), 150 MM NACL, 10 MM KCL, 10 MM MGCL2, 20 MM NA2MOO4, 2MM DTT, 0.085MM DDM;pH 7.5;20MM TRIS-HCL (PH 7.5), 150 MM NACL, 10 MM KCL, 10 MM MGCL2, 20 MM NA2MOO4, 2MM DTT, 0.085MM DDM cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 8.00 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.

14 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDK4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 8–310; UniProt 1–303

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 5fwm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fwm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fwm
Deposition date deposition_date2016-02-18
Structure title titleAtomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex
Keywords keywordsHSP90, CDC37, CDK4, CHAPERONE, KINASE, UNFOLDING; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.40
Radius of gyration Rg (electron density) rg_electron39.74
Forward intensity I(0) i0660524000.00
Molecular weight molecular_weight210790.0 kDa
Excluded volume excluded_volume264100 ų
Envelope volume envelope_volume340080 ų
Hydration-shell volume shell_volume70096 ų
Envelope diameter envelope_diameter153.5
Shell Rg shell_rg46.34
Envelope Rg envelope_rg39.44
Shape Rg shape_rg39.72
Total Rg total_rg40.14
Total atoms total_atoms29596
Residues n_residues1817
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 dmax145.5
Rg (real space) rg_real40.29
Rg uncertainty (real space) rg_real_error1.48
I(0) (real space) i0_real6.6050e+08
I(0) uncertainty (real space) i0_real_error1.3450e+07
Rg (reciprocal space) rg_reciprocal40.40
I(0) (reciprocal space) i0_reciprocal660600000.0000
Solution quality estimate total_estimate0.8467
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.2
Skewness Skewness skewness0.273
Kurtosis Kurtosis kurtosis-0.234
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha95100000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.673; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)