9ync

Motor domains of phi-like human dynein-1 bound to dynactin-p150glued and LIS1

Method: ELECTRON MICROSCOPY Dmax: 230.8 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–4646 Chain B; UniProt 1–4646 Not recorded Platelet-activating factor acetylhydrolase IB subunit beta × 4 (P43034) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 B; 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 1–410 Chain D; UniProt 1–410 Chain E; UniProt 1–410 Chain F; UniProt 1–410 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 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 F; PDBConstruct 1–410; UniProt 1–410

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain G; UniProt 1–638 Chain H; UniProt 1–638 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Platelet-activating factor acetylhydrolase IB subunit beta × 4 (P43034) Dynactin subunit 1 × 2 (A0A287B8J2) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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
PDB entities 3
Chains and sequence ranges Author chain G; PDBConstruct 1–638; UniProt 1–638 Author chain H; PDBConstruct 1–638; UniProt 1–638

Dynactin subunit 1

Sus scrofa

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain I; UniProt 1–1278 Chain J; UniProt 1–1278 Not recorded Cytoplasmic dynein 1 heavy chain 1 × 2 (Q14204) Platelet-activating factor acetylhydrolase IB subunit beta × 4 (P43034) Cytoplasmic dynein 1 intermediate chain 2 × 2 (Q13409) ADP ADENOSINE-5'-DIPHOSPHATE × 6 ATP ADENOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.93 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 1–1278; UniProt 1–1278 Author chain J; PDBConstruct 1–1278; UniProt 1–1278

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 9ync

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ync
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ync
Deposition date deposition_date2025-10-10
Structure title titleMotor domains of phi-like human dynein-1 bound to dynactin-p150glued and LIS1
Keywords keywordsDynein-1, phi-like conformation, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.10
Radius of gyration Rg (electron density) rg_electron66.71
Forward intensity I(0) i09101800000.00
Molecular weight molecular_weight808160.0 kDa
Excluded volume excluded_volume1011200 ų
Envelope volume envelope_volume1565900 ų
Hydration-shell volume shell_volume188550 ų
Envelope diameter envelope_diameter261.8
Shell Rg shell_rg72.77
Envelope Rg envelope_rg65.43
Shape Rg shape_rg66.72
Total Rg total_rg66.77
Total atoms total_atoms56877
Residues n_residues7224
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 dmax230.8
Rg (real space) rg_real66.94
Rg uncertainty (real space) rg_real_error1.86
I(0) (real space) i0_real9.1020e+09
I(0) uncertainty (real space) i0_real_error2.0460e+08
Rg (reciprocal space) rg_reciprocal67.56
I(0) (reciprocal space) i0_reciprocal9111000000.0000
Solution quality estimate total_estimate0.8645
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary80.3
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0005
Highest regularization parameter α highest_alpha931200000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.792; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.879

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)