9dnb

CryoEM structures of yeast cytoplasmic dynein in the presence of ATP and Lis1.

Method: ELECTRON MICROSCOPY Dmax: 174.8 Å Quality: GOOD

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

Dynein heavy chain, cytoplasmic

Saccharomyces cerevisiae

UniProt P36022

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1219–4092 Not recorded Nuclear distribution protein PAC1 × 2 (P39946) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;50 mM TrisHCl [pH 8.0], 150 mM KOAc, 2 mM MgOAc, 1mM EGTA, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

39 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DYHC_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–2875; UniProt 1219–4092

Nuclear distribution protein PAC1

Saccharomyces cerevisiae

UniProt P39946

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–494 Chain C; UniProt 1–494 Not recorded Dynein heavy chain, cytoplasmic × 1 (P36022) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;50 mM TrisHCl [pH 8.0], 150 mM KOAc, 2 mM MgOAc, 1mM EGTA, 1 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LIS1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–495; UniProt 1–494 Author chain C; PDBConstruct 2–495; UniProt 1–494

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 9dnb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9dnb
Deposition date deposition_date2024-09-17
Structure title titleCryoEM structures of yeast cytoplasmic dynein in the presence of ATP and Lis1.
Keywords keywordsEnzyme, AAA protein, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier51.58
Radius of gyration Rg (electron density) rg_electron51.07
Forward intensity I(0) i01490980000.00
Molecular weight molecular_weight325380.0 kDa
Excluded volume excluded_volume407880 ų
Envelope volume envelope_volume581040 ų
Hydration-shell volume shell_volume92466 ų
Envelope diameter envelope_diameter179.1
Shell Rg shell_rg56.21
Envelope Rg envelope_rg50.79
Shape Rg shape_rg51.14
Total Rg total_rg50.96
Total atoms total_atoms22963
Residues n_residues3020
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 dmax174.8
Rg (real space) rg_real51.59
Rg uncertainty (real space) rg_real_error1.46
I(0) (real space) i0_real1.4910e+09
I(0) uncertainty (real space) i0_real_error2.7690e+07
Rg (reciprocal space) rg_reciprocal51.55
I(0) (reciprocal space) i0_reciprocal1491000000.0000
Solution quality estimate total_estimate0.8763
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.0
Skewness Skewness skewness0.345
Kurtosis Kurtosis kurtosis-0.348
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha185500000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.796

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)