9bmz

State-2 of motor domain from full-length human dynein-1 in apo condition

Method: ELECTRON MICROSCOPY Dmax: 192.5 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–4646 Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2;25 mM HEPES pH 7.2, 150 mM KCl, 1 mM MgCl2, 5 mM DTT cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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

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 9bmz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9bmz
Deposition date deposition_date2024-05-02
Structure title titleState-2 of motor domain from full-length human dynein-1 in apo condition
Keywords keywordsdynein-1, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.83
Radius of gyration Rg (electron density) rg_electron48.68
Forward intensity I(0) i01607600000.00
Molecular weight molecular_weight336990.0 kDa
Excluded volume excluded_volume423190 ų
Envelope volume envelope_volume579090 ų
Hydration-shell volume shell_volume97831 ų
Envelope diameter envelope_diameter209.3
Shell Rg shell_rg54.60
Envelope Rg envelope_rg48.19
Shape Rg shape_rg48.67
Total Rg total_rg48.92
Total atoms total_atoms23707
Residues n_residues2937
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 dmax192.5
Rg (real space) rg_real48.93
Rg uncertainty (real space) rg_real_error2.11
I(0) (real space) i0_real1.6080e+09
I(0) uncertainty (real space) i0_real_error3.4800e+07
Rg (reciprocal space) rg_reciprocal48.83
I(0) (reciprocal space) i0_reciprocal1607000000.0000
Solution quality estimate total_estimate0.7910
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.2
Skewness Skewness skewness0.557
Kurtosis Kurtosis kurtosis0.590
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha220700000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.451; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.955

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)