8sh7

TUBB4B and TUBA1A Heterodimer from Human Respiratory Doublet Microtubules

Method: ELECTRON MICROSCOPY Dmax: 102.2 Å Quality: GOOD

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

Tubulin alpha-1A chain

OrganismNot specified

UniProt Q71U36

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–451 Not recorded Tubulin beta-4B chain × 1 (P68371) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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 TBA1A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 1–451

Tubulin beta-4B chain

OrganismNot specified

UniProt P68371

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–445 Not recorded Tubulin alpha-1A chain × 1 (Q71U36) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB4B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 1–445

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 8sh7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8sh7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8sh7
Deposition date deposition_date2023-04-13
Structure title titleTUBB4B and TUBA1A Heterodimer from Human Respiratory Doublet Microtubules
Keywords keywordsCilia, Axoneme, Microtubule, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.50
Radius of gyration Rg (electron density) rg_electron29.85
Forward intensity I(0) i0157249000.00
Molecular weight molecular_weight97189.0 kDa
Excluded volume excluded_volume120360 ų
Envelope volume envelope_volume147030 ų
Hydration-shell volume shell_volume40780 ų
Envelope diameter envelope_diameter107.3
Shell Rg shell_rg37.48
Envelope Rg envelope_rg30.13
Shape Rg shape_rg29.87
Total Rg total_rg30.43
Total atoms total_atoms6819
Residues n_residues862
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 dmax102.2
Rg (real space) rg_real30.54
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real1.5720e+08
I(0) uncertainty (real space) i0_real_error2.3580e+06
Rg (reciprocal space) rg_reciprocal30.52
I(0) (reciprocal space) i0_reciprocal157200000.0000
Solution quality estimate total_estimate0.8718
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.431
Kurtosis Kurtosis kurtosis-0.273
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha52870000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.934

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)