8pr0

Cytoplasmic dynein-A heavy chain bound to dynactin-p150glued and IC-LC tower

Method: ELECTRON MICROSCOPY Dmax: 214.2 Å Quality: GOOD

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

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain C; UniProt 1–612 Chain D; UniProt 1–612 Not recorded Dynein light chain 1, cytoplasmic × 2 (P63167) Dynein light chain Tctex-type 1 × 2 (P63172) Dynactin subunit 1 × 2 (A0A287B8J2) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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 1
Chains and sequence ranges Author chain C; PDBConstruct 1–612; UniProt 1–612 Author chain D; PDBConstruct 1–612; UniProt 1–612

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain E; UniProt 1–89 Chain F; UniProt 1–89 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain Tctex-type 1 × 2 (P63172) Dynactin subunit 1 × 2 (A0A287B8J2) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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 2
Chains and sequence ranges Author chain E; PDBConstruct 1–89; UniProt 1–89 Author chain F; 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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain G; UniProt 1–113 Chain H; UniProt 1–113 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain 1, cytoplasmic × 2 (P63167) Dynactin subunit 1 × 2 (A0A287B8J2) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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 3
Chains and sequence ranges Author chain G; PDBConstruct 1–113; UniProt 1–113 Author chain H; PDBConstruct 1–113; UniProt 1–113

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain I; UniProt 1–1281 Chain J; UniProt 1–1281 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain 1, cytoplasmic × 2 (P63167) Dynein light chain Tctex-type 1 × 2 (P63172) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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 4
Chains and sequence ranges Author chain I; PDBConstruct 1–1281; UniProt 1–1281 Author chain J; PDBConstruct 1–1281; UniProt 1–1281

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain A; UniProt 1–4646 Chain B; UniProt 1–4646 Mutation:R1567E, K1610E Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain 1, cytoplasmic × 2 (P63167) Dynein light chain Tctex-type 1 × 2 (P63172) Dynactin subunit 1 × 2 (A0A287B8J2) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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 5
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 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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain K; UniProt 1–492 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain 1, cytoplasmic × 2 (P63167) Dynein light chain Tctex-type 1 × 2 (P63172) Dynactin subunit 1 × 2 (A0A287B8J2) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 9.40 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 6
Chains and sequence ranges Author chain K; PDBConstruct 1–492; UniProt 1–492

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 8pr0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pr0
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8pr0
Deposition date deposition_date2023-07-12
Structure title titleCytoplasmic dynein-A heavy chain bound to dynactin-p150glued and IC-LC tower
Keywords keywordsDynein, AAA-Atpase, dynactin, p150, LC8, TCTEX1, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.39
Radius of gyration Rg (electron density) rg_electron62.69
Forward intensity I(0) i0724252000.00
Molecular weight molecular_weight183720.0 kDa
Excluded volume excluded_volume211970 ų
Envelope volume envelope_volume542650 ų
Hydration-shell volume shell_volume78325 ų
Envelope diameter envelope_diameter243.6
Shell Rg shell_rg59.43
Envelope Rg envelope_rg58.46
Shape Rg shape_rg62.69
Total Rg total_rg62.57
Total atoms total_atoms13123
Residues n_residues2649
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 dmax214.2
Rg (real space) rg_real62.47
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real7.2410e+08
I(0) uncertainty (real space) i0_real_error1.5410e+07
Rg (reciprocal space) rg_reciprocal62.26
I(0) (reciprocal space) i0_reciprocal723900000.0000
Solution quality estimate total_estimate0.8707
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary85.7
Skewness Skewness skewness0.297
Kurtosis Kurtosis kurtosis-0.237
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0037
Highest regularization parameter α highest_alpha44440000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.704

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)