8pr4

Dynactin pointed end bound to JIP3

Method: ELECTRON MICROSCOPY Dmax: 112.4 Å Quality: GOOD

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

Arp11

OrganismNot specified

UniProt I3LHK5

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 1–417 Not recorded Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) C-Jun-amino-terminal kinase-interacting protein 3 × 2 (Q9UPT6) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name I3LHK5_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain J; PDBConstruct 1–417; UniProt 1–417

Dynactin 6

OrganismNot specified

UniProt D0G6S1

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 U; UniProt 1–190 Not recorded Arp11 × 1 (I3LHK5) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) C-Jun-amino-terminal kinase-interacting protein 3 × 2 (Q9UPT6) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name D0G6S1_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain U; PDBConstruct 1–190; UniProt 1–190

Dynactin subunit 5

OrganismNot specified

UniProt A0A286ZK88

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 W; UniProt 1–182 Not recorded Arp11 × 1 (I3LHK5) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 4 × 1 (A0A4X1TB62) C-Jun-amino-terminal kinase-interacting protein 3 × 2 (Q9UPT6) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A286ZK88_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain W; PDBConstruct 1–182; UniProt 1–182

Dynactin subunit 4

OrganismNot specified

UniProt A0A4X1TB62

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 Y; UniProt 1–467 Not recorded Arp11 × 1 (I3LHK5) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) C-Jun-amino-terminal kinase-interacting protein 3 × 2 (Q9UPT6) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4X1TB62_PIG
Isoform
PDB entities 4
Chains and sequence ranges Author chain Y; PDBConstruct 1–467; UniProt 1–467

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 X; UniProt 1–560 Chain x; UniProt 1–560 Not recorded Arp11 × 1 (I3LHK5) Dynactin 6 × 1 (D0G6S1) Dynactin subunit 5 × 1 (A0A286ZK88) Dynactin subunit 4 × 1 (A0A4X1TB62) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 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.

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 5
Chains and sequence ranges Author chain X; PDBConstruct 8–567; UniProt 1–560 Author chain x; PDBConstruct 8–567; UniProt 1–560

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 8pr4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pr4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8pr4
Deposition date deposition_date2023-07-12
Structure title titleDynactin pointed end bound to JIP3
Keywords keywordsDynein, AAA-Atpase, p150, 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_guinier35.69
Radius of gyration Rg (electron density) rg_electron34.83
Forward intensity I(0) i0289044000.00
Molecular weight molecular_weight135170.0 kDa
Excluded volume excluded_volume168570 ų
Envelope volume envelope_volume239490 ų
Hydration-shell volume shell_volume55716 ų
Envelope diameter envelope_diameter122.7
Shell Rg shell_rg42.62
Envelope Rg envelope_rg34.65
Shape Rg shape_rg34.89
Total Rg total_rg35.21
Total atoms total_atoms9494
Residues n_residues1322
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 dmax112.4
Rg (real space) rg_real35.52
Rg uncertainty (real space) rg_real_error0.81
I(0) (real space) i0_real2.8900e+08
I(0) uncertainty (real space) i0_real_error4.7940e+06
Rg (reciprocal space) rg_reciprocal35.63
I(0) (reciprocal space) i0_reciprocal289100000.0000
Solution quality estimate total_estimate0.8986
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.0
Skewness Skewness skewness0.173
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha66450000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.913

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)