6rza

Cryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules

Method: ELECTRON MICROSCOPY Dmax: 129.8 Å Quality: REASONABLE

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

Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain 7, axonemal,Cytoplasmic dynein 1 heavy chain 1

Mus musculus

UniProt Q8WXX0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain X; UniProt 2674–2812 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (P02554) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DYH7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 16–154; UniProt 2674–2812

Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain 7, axonemal,Cytoplasmic dynein 1 heavy chain 1

Mus musculus

UniProt Q9JHU4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain X; UniProt 3270–3284 Chain X; UniProt 3410–3418 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (P02554) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

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

View Construct and Data Evidence
UniProt name DYHC1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain X; PDBConstruct 1–15; UniProt 3270–3284 Author chain X; PDBConstruct 155–163; UniProt 3410–3418

Tubulin alpha-1B chain

OrganismNot specified

UniProt Q2XVP4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–437 Chain C; UniProt 1–437 Not recorded Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain 7, axonemal,Cytoplasmic dynein 1 heavy chain 1 × 1 (Q9JHU4,Q8WXX0) Tubulin beta chain × 2 (P02554) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

230 other PDB entries and 243 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1B_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–437; UniProt 1–437 Author chain C; PDBConstruct 1–437; UniProt 1–437

Tubulin beta chain

OrganismNot specified

UniProt P02554

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–426 Chain D; UniProt 1–426 Not recorded Cytoplasmic dynein 1 heavy chain 1,Dynein heavy chain 7, axonemal,Cytoplasmic dynein 1 heavy chain 1 × 1 (Q9JHU4,Q8WXX0) Tubulin alpha-1B chain × 2 (Q2XVP4) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 TA1 TAXOL × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.50 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.

137 other PDB entries and 159 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–426; UniProt 1–426 Author chain D; PDBConstruct 1–426; UniProt 1–426

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 6rza

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6rza
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6rza
Deposition date deposition_date2019-06-13
Structure title titleCryo-EM structure of the human inner arm dynein DNAH7 microtubule binding domain bound to microtubules
Keywords keywordsfilament, complex, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.22
Radius of gyration Rg (electron density) rg_electron39.72
Forward intensity I(0) i0690968000.00
Molecular weight molecular_weight212450.0 kDa
Excluded volume excluded_volume264070 ų
Envelope volume envelope_volume327240 ų
Hydration-shell volume shell_volume66444 ų
Envelope diameter envelope_diameter139.7
Shell Rg shell_rg47.16
Envelope Rg envelope_rg39.39
Shape Rg shape_rg39.73
Total Rg total_rg40.07
Total atoms total_atoms14908
Residues n_residues1867
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 dmax129.8
Rg (real space) rg_real40.10
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real6.9100e+08
I(0) uncertainty (real space) i0_real_error1.2350e+07
Rg (reciprocal space) rg_reciprocal40.22
I(0) (reciprocal space) i0_reciprocal691000000.0000
Solution quality estimate total_estimate0.6690
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.2
Skewness Skewness skewness0.184
Kurtosis Kurtosis kurtosis-0.502
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha170300000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 0.025; Positv: 1.000; Valcen: 1.000; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)