8pr1

Cytoplasmic dynein-B heavy chain bound to IC-LC tower

Method: ELECTRON MICROSCOPY Dmax: 216.8 Å Quality: GOOD

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

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 D; UniProt 1–89 Chain E; UniProt 1–89 Not recorded Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain Tctex-type 1 × 2 (P63172) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 1
Chains and sequence ranges Author chain D; PDBConstruct 1–89; UniProt 1–89 Author chain E; PDBConstruct 1–89; UniProt 1–89

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 I; UniProt 1–612 Chain J; UniProt 1–612 Not recorded 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 × 2 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 2
Chains and sequence ranges Author chain I; PDBConstruct 1–612; UniProt 1–612 Author chain J; PDBConstruct 1–612; UniProt 1–612

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 Dynein light chain 1, cytoplasmic × 2 (P63167) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 K; PDBConstruct 1–113; UniProt 1–113 Author chain L; PDBConstruct 1–113; UniProt 1–113

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 G; UniProt 1–4646 Mutation:R1567E, K1610E Dynein light chain 1, cytoplasmic × 2 (P63167) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain Tctex-type 1 × 2 (P63172) Cytoplasmic dynein 1 light intermediate chain 2 × 2 (O43237) Dynein light chain roadblock-type 1 × 2 (Q9NP97) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 4
Chains and sequence ranges Author chain A; PDBConstruct 1–4646; UniProt 1–4646 Author chain G; 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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain F; UniProt 1–492 Chain H; UniProt 1–492 Not recorded Dynein light chain 1, cytoplasmic × 2 (P63167) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain Tctex-type 1 × 2 (P63172) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Dynein light chain roadblock-type 1 × 2 (Q9NP97) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 5
Chains and sequence ranges Author chain F; PDBConstruct 1–492; UniProt 1–492 Author chain H; 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 s; UniProt 1–96 Chain t; UniProt 1–96 Not recorded Dynein light chain 1, cytoplasmic × 2 (P63167) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynein light chain Tctex-type 1 × 2 (P63172) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 light intermediate chain 2 × 2 (O43237) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.20 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 6
Chains and sequence ranges Author chain s; PDBConstruct 1–96; UniProt 1–96 Author chain t; PDBConstruct 1–96; UniProt 1–96

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 8pr1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pr1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8pr1
Deposition date deposition_date2023-07-12
Structure title titleCytoplasmic dynein-B heavy chain bound to IC-LC tower
Keywords keywordsDynein, AAA-Atpase, 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_guinier76.85
Radius of gyration Rg (electron density) rg_electron77.79
Forward intensity I(0) i01325330000.00
Molecular weight molecular_weight250040.0 kDa
Excluded volume excluded_volume287710 ų
Envelope volume envelope_volume783950 ų
Hydration-shell volume shell_volume91064 ų
Envelope diameter envelope_diameter280.4
Shell Rg shell_rg66.42
Envelope Rg envelope_rg74.63
Shape Rg shape_rg77.77
Total Rg total_rg77.59
Total atoms total_atoms17871
Residues n_residues3611
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 dmax216.8
Rg (real space) rg_real74.95
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real1.3050e+09
I(0) uncertainty (real space) i0_real_error2.4640e+07
Rg (reciprocal space) rg_reciprocal74.53
I(0) (reciprocal space) i0_reciprocal1317000000.0000
Solution quality estimate total_estimate0.8484
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.9
Skewness Skewness skewness0.379
Kurtosis Kurtosis kurtosis-0.670
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.0790
Highest regularization parameter α highest_alpha73170000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.975; Stabil: 0.987; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.004

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)