8pqz

Cytoplasmic dynein-1 A1/A2 motor domains bound to LIS1

Method: ELECTRON MICROSCOPY Dmax: 264.9 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 J; UniProt 1–4646 Mutation:R1567E, K1610E Platelet-activating factor acetylhydrolase IB subunit beta × 6 (P43034) Dynactin subunit 1 × 2 (A0A287B8J2) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 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 J; PDBConstruct 1–4646; UniProt 1–4646

Platelet-activating factor acetylhydrolase IB subunit beta

Homo sapiens

UniProt P43034

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 B; UniProt 1–410 Chain C; UniProt 1–410 Chain D; UniProt 1–410 Chain E; UniProt 1–410 Chain K; UniProt 1–410 Chain L; UniProt 1–410 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Dynactin subunit 1 × 2 (A0A287B8J2) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LIS1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–410; UniProt 1–410 Author chain C; PDBConstruct 1–410; UniProt 1–410 Author chain D; PDBConstruct 1–410; UniProt 1–410 Author chain E; PDBConstruct 1–410; UniProt 1–410 Author chain K; PDBConstruct 1–410; UniProt 1–410 Author chain L; PDBConstruct 1–410; UniProt 1–410

Dynactin subunit 1

OrganismNot specified

UniProt A0A287B8J2

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 F; UniProt 1–1281 Chain G; UniProt 1–1281 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Platelet-activating factor acetylhydrolase IB subunit beta × 6 (P43034) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DCTN1_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–1281; UniProt 1–1281 Author chain G; PDBConstruct 1–1281; UniProt 1–1281

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 H; UniProt 1–612 Chain I; UniProt 1–612 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Platelet-activating factor acetylhydrolase IB subunit beta × 6 (P43034) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 4 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.50 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 Q13409-3
PDB entities 4
Chains and sequence ranges Author chain H; PDBConstruct 1–612; UniProt 1–612 Author chain I; PDBConstruct 1–612; UniProt 1–612

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 8pqz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8pqz
Deposition date deposition_date2023-07-12
Structure title titleCytoplasmic dynein-1 A1/A2 motor domains bound to LIS1
Keywords keywordsDynein, AAA-Atpase, LIS1, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier71.81
Radius of gyration Rg (electron density) rg_electron71.77
Forward intensity I(0) i05864410000.00
Molecular weight molecular_weight527130.0 kDa
Excluded volume excluded_volume605630 ų
Envelope volume envelope_volume1527400 ų
Hydration-shell volume shell_volume175470 ų
Envelope diameter envelope_diameter268.8
Shell Rg shell_rg74.90
Envelope Rg envelope_rg68.52
Shape Rg shape_rg71.76
Total Rg total_rg71.83
Total atoms total_atoms37643
Residues n_residues7553
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 dmax264.9
Rg (real space) rg_real75.46
Rg uncertainty (real space) rg_real_error1.59
I(0) (real space) i0_real5.8930e+09
I(0) uncertainty (real space) i0_real_error1.1700e+08
Rg (reciprocal space) rg_reciprocal72.43
I(0) (reciprocal space) i0_reciprocal5873000000.0000
Solution quality estimate total_estimate0.8953
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.3
Skewness Skewness skewness0.488
Kurtosis Kurtosis kurtosis0.255
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.9446
Highest regularization parameter α highest_alpha890400000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.759; Stabil: 0.862; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.847

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)