8pr2

Cytoplasmic dynein-1 heavy chain bound to JIP3-LZI

Method: ELECTRON MICROSCOPY Dmax: 196.9 Å Quality: REASONABLE

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

C-Jun-amino-terminal kinase-interacting protein 3

Homo sapiens

UniProt Q9UPT6

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–560 Chain C; UniProt 1–560 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 1 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name JIP3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 8–567; UniProt 1–560 Author chain C; PDBConstruct 8–567; UniProt 1–560

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain f; UniProt 1–4646 Chain m; UniProt 1–4646 Mutation:R1567E, K1610E C-Jun-amino-terminal kinase-interacting protein 3 × 2 (Q9UPT6) Cytoplasmic dynein 1 intermediate chain 2 × 1 (Q13409) Cytoplasmic dynein 1 light intermediate chain 2 × 1 (O43237) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 2
Chains and sequence ranges Author chain f; PDBConstruct 1–4646; UniProt 1–4646 Author chain m; 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain h; UniProt 1–612 Not recorded C-Jun-amino-terminal kinase-interacting protein 3 × 2 (Q9UPT6) 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 3.80 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 3
Chains and sequence ranges Author chain h; PDBConstruct 1–612; UniProt 1–612

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain j; UniProt 1–492 Not recorded C-Jun-amino-terminal kinase-interacting protein 3 × 2 (Q9UPT6) Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 1 (Q13409) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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 4
Chains and sequence ranges Author chain j; 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 8pr2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pr2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8pr2
Deposition date deposition_date2023-07-12
Structure title titleCytoplasmic dynein-1 heavy chain bound to JIP3-LZI
Keywords keywordsDynein, AAA-Atpase, JIP3, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.67
Radius of gyration Rg (electron density) rg_electron50.33
Forward intensity I(0) i0667954000.00
Molecular weight molecular_weight211520.0 kDa
Excluded volume excluded_volume264480 ų
Envelope volume envelope_volume408630 ų
Hydration-shell volume shell_volume71794 ų
Envelope diameter envelope_diameter212.3
Shell Rg shell_rg49.67
Envelope Rg envelope_rg50.30
Shape Rg shape_rg50.31
Total Rg total_rg50.37
Total atoms total_atoms14906
Residues n_residues1816
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 dmax196.9
Rg (real space) rg_real50.19
Rg uncertainty (real space) rg_real_error3.26
I(0) (real space) i0_real6.6800e+08
I(0) uncertainty (real space) i0_real_error1.5150e+07
Rg (reciprocal space) rg_reciprocal49.67
I(0) (reciprocal space) i0_reciprocal667500000.0000
Solution quality estimate total_estimate0.7206
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary55.4
Skewness Skewness skewness0.641
Kurtosis Kurtosis kurtosis0.304
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha54360000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.511; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.831; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)