9bly

Composite structure of full-length human dynein-1 in phi-particle conformation

Method: ELECTRON MICROSCOPY Dmax: 426.7 Å Quality: GOOD

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

Cytoplasmic dynein 1 heavy chain 1

Homo sapiens

UniProt Q14204

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain A; UniProt 1–4646 Chain B; UniProt 1–4646 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 2 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynein light chain 1, cytoplasmic × 2 (P63167) Dynein light chain Tctex-type 1 × 2 (P63172) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

96 other PDB entries and 97 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DYHC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–4646; UniProt 1–4646 Author chain B; PDBConstruct 1–4646; UniProt 1–4646

Cytoplasmic dynein 1 intermediate chain 2

Homo sapiens

UniProt Q13409

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain C; UniProt 1–638 Chain D; UniProt 1–638 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 2 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynein light chain 1, cytoplasmic × 2 (P63167) Dynein light chain Tctex-type 1 × 2 (P63172) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DC1I2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–638; UniProt 1–638 Author chain D; PDBConstruct 1–638; UniProt 1–638

Cytoplasmic dynein 1 light intermediate chain 2

Homo sapiens

UniProt O43237

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain E; UniProt 1–492 Chain F; UniProt 1–492 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynein light chain 1, cytoplasmic × 2 (P63167) Dynein light chain Tctex-type 1 × 2 (P63172) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DC1L2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–492; UniProt 1–492 Author chain F; PDBConstruct 1–492; UniProt 1–492

Dynein light chain roadblock-type 1

Homo sapiens

UniProt Q9NP97

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain G; UniProt 1–96 Chain H; UniProt 1–96 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 2 (O43237) Dynein light chain 1, cytoplasmic × 2 (P63167) Dynein light chain Tctex-type 1 × 2 (P63172) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

23 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DLRB1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–96; UniProt 1–96 Author chain H; PDBConstruct 1–96; UniProt 1–96

Dynein light chain 1, cytoplasmic

Homo sapiens

UniProt P63167

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain I; UniProt 1–89 Chain J; UniProt 1–89 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 2 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynein light chain Tctex-type 1 × 2 (P63172) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

20 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DYL1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain I; PDBConstruct 1–89; UniProt 1–89 Author chain J; PDBConstruct 1–89; UniProt 1–89

Dynein light chain Tctex-type 1

Homo sapiens

UniProt P63172

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain K; UniProt 1–113 Chain L; UniProt 1–113 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 2 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) Dynein light chain 1, cytoplasmic × 2 (P63167) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT, 5 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DYLT1_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain K; PDBConstruct 1–113; UniProt 1–113 Author chain L; PDBConstruct 1–113; UniProt 1–113

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 9bly

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bly
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9bly
Deposition date deposition_date2024-05-02
Structure title titleComposite structure of full-length human dynein-1 in phi-particle conformation
Keywords keywordsdynein-1, phi-particle, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron158.40
Forward intensity I(0) i021641200000.00
Molecular weight molecular_weight1270300.0 kDa
Excluded volume excluded_volume1594900 ų
Envelope volume envelope_volume3497100 ų
Hydration-shell volume shell_volume204170 ų
Envelope diameter envelope_diameter624.9
Shell Rg shell_rg103.30
Envelope Rg envelope_rg160.30
Shape Rg shape_rg158.40
Total Rg total_rg158.30
Total atoms total_atoms89391
Residues n_residues11063
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 dmax426.7
Rg (real space) rg_real142.70
Rg uncertainty (real space) rg_real_error3.38
I(0) (real space) i0_real2.0660e+10
I(0) uncertainty (real space) i0_real_error5.5000e+08
Rg (reciprocal space) rg_reciprocal105.90
I(0) (reciprocal space) i0_reciprocal18500000000.0000
Solution quality estimate total_estimate0.8288
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary85.3
Skewness Skewness skewness0.446
Kurtosis Kurtosis kurtosis-0.924
Angular range angular_range— – 0.0500 −1
Current regularization parameter α current_alpha0.8802
Highest regularization parameter α highest_alpha380400000.0000
Real-space data points n_real_points11
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.127; Oscil: 0.678; Stabil: 0.962; Sysdev: 1.000; Positv: 1.000; Valcen: 0.855; Smooth: 0.007

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)