9t1d

Cryo-EM reconstruction of undecorated GDP microtubule

Method: ELECTRON MICROSCOPY Dmax: 98.7 Å Quality: REASONABLE

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

Detyrosinated tubulin alpha-1A chain

OrganismNot specified

UniProt P02550

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 1–439 Not recorded Tubulin beta chain × 1 (P02554) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.90 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 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1A_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–439; UniProt 1–439

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 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–429 Not recorded Detyrosinated tubulin alpha-1A chain × 1 (P02550) GTP GUANOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.90 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–429; UniProt 1–429

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 9t1d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t1d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9t1d
Deposition date deposition_date2025-10-21
Structure title titleCryo-EM reconstruction of undecorated GDP microtubule
Keywords keywordsMicrotubule. Tubulin dimer., STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.72
Radius of gyration Rg (electron density) rg_electron29.08
Forward intensity I(0) i0153640000.00
Molecular weight molecular_weight96114.0 kDa
Excluded volume excluded_volume119050 ų
Envelope volume envelope_volume141450 ų
Hydration-shell volume shell_volume40030 ų
Envelope diameter envelope_diameter106.3
Shell Rg shell_rg36.99
Envelope Rg envelope_rg29.42
Shape Rg shape_rg29.09
Total Rg total_rg29.68
Total atoms total_atoms6746
Residues n_residues852
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 dmax98.7
Rg (real space) rg_real29.74
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.5360e+08
I(0) uncertainty (real space) i0_real_error2.1690e+06
Rg (reciprocal space) rg_reciprocal29.74
I(0) (reciprocal space) i0_reciprocal153600000.0000
Solution quality estimate total_estimate0.6558
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.5
Skewness Skewness skewness0.425
Kurtosis Kurtosis kurtosis-0.260
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51410000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.818; Stabil: 1.000; Sysdev: 0.050; Positv: 1.000; Valcen: 0.994; Smooth: 0.922

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)