6o2t

Acetylated Microtubules

Method: ELECTRON MICROSCOPY Dmax: 397.5 Å Quality: GOOD

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

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 Protein heterocomplex Heteromer Protein × 104 PDB declaration: 104-meric(104) Consistent with protein copy count Chain 1A; UniProt 1–451 Chain 1B; UniProt 1–451 Chain 1C; UniProt 1–451 Chain 1D; UniProt 1–451 Chain 1E; UniProt 1–451 Chain 1F; UniProt 1–451 Chain 1G; UniProt 1–451 Chain 1I; UniProt 1–451 Chain 1J; UniProt 1–451 Chain 1K; UniProt 1–451 Chain 1L; UniProt 1–451 Chain 1M; UniProt 1–451 Chain 1N; UniProt 1–451 Chain 2A; UniProt 1–451 Chain 2B; UniProt 1–451 Chain 2C; UniProt 1–451 Chain 2D; UniProt 1–451 Chain 2E; UniProt 1–451 Chain 2F; UniProt 1–451 Chain 2G; UniProt 1–451 Chain 2I; UniProt 1–451 Chain 2J; UniProt 1–451 Chain 2K; UniProt 1–451 Chain 2L; UniProt 1–451 Chain 2M; UniProt 1–451 Chain 2N; UniProt 1–451 Chain 3A; UniProt 1–451 Chain 3B; UniProt 1–451 Chain 3C; UniProt 1–451 Chain 3D; UniProt 1–451 Chain 3E; UniProt 1–451 Chain 3F; UniProt 1–451 Chain 3G; UniProt 1–451 Chain 3I; UniProt 1–451 Chain 3J; UniProt 1–451 Chain 3K; UniProt 1–451 Chain 3L; UniProt 1–451 Chain 3M; UniProt 1–451 Chain 3N; UniProt 1–451 Chain 4A; UniProt 1–451 Chain 4B; UniProt 1–451 Chain 4C; UniProt 1–451 Chain 4D; UniProt 1–451 Chain 4E; UniProt 1–451 Chain 4F; UniProt 1–451 Chain 4G; UniProt 1–451 Chain 4I; UniProt 1–451 Chain 4J; UniProt 1–451 Chain 4K; UniProt 1–451 Chain 4L; UniProt 1–451 Chain 4M; UniProt 1–451 Chain 4N; UniProt 1–451 Not recorded Tubulin beta chain × 52 (P02554) GTP GUANOSINE-5'-TRIPHOSPHATE × 52 MG MAGNESIUM ION × 52 GDP GUANOSINE-5'-DIPHOSPHATE × 52 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8;Contains 80 mM PIPES, 1 mM MgCl2, 1 mM EGTA, pH 6.8 with KOH (stored at 4 degrees Celsius). cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 4 seconds at blot force 10. Resolution 4.10 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 1
Chains and sequence ranges Author chain 1A; PDBConstruct 1–451; UniProt 1–451 Author chain 1B; PDBConstruct 1–451; UniProt 1–451 Author chain 1C; PDBConstruct 1–451; UniProt 1–451 Author chain 1D; PDBConstruct 1–451; UniProt 1–451 Author chain 1E; PDBConstruct 1–451; UniProt 1–451 Author chain 1F; PDBConstruct 1–451; UniProt 1–451 Author chain 1G; PDBConstruct 1–451; UniProt 1–451 Author chain 1I; PDBConstruct 1–451; UniProt 1–451 Author chain 1J; PDBConstruct 1–451; UniProt 1–451 Author chain 1K; PDBConstruct 1–451; UniProt 1–451 Author chain 1L; PDBConstruct 1–451; UniProt 1–451 Author chain 1M; PDBConstruct 1–451; UniProt 1–451 Author chain 1N; PDBConstruct 1–451; UniProt 1–451 Author chain 2A; PDBConstruct 1–451; UniProt 1–451 Author chain 2B; PDBConstruct 1–451; UniProt 1–451 Author chain 2C; PDBConstruct 1–451; UniProt 1–451 Author chain 2D; PDBConstruct 1–451; UniProt 1–451 Author chain 2E; PDBConstruct 1–451; UniProt 1–451 Author chain 2F; PDBConstruct 1–451; UniProt 1–451 Author chain 2G; PDBConstruct 1–451; UniProt 1–451 Author chain 2I; PDBConstruct 1–451; UniProt 1–451 Author chain 2J; PDBConstruct 1–451; UniProt 1–451 Author chain 2K; PDBConstruct 1–451; UniProt 1–451 Author chain 2L; PDBConstruct 1–451; UniProt 1–451 Author chain 2M; PDBConstruct 1–451; UniProt 1–451 Author chain 2N; PDBConstruct 1–451; UniProt 1–451 Author chain 3A; PDBConstruct 1–451; UniProt 1–451 Author chain 3B; PDBConstruct 1–451; UniProt 1–451 Author chain 3C; PDBConstruct 1–451; UniProt 1–451 Author chain 3D; PDBConstruct 1–451; UniProt 1–451 Author chain 3E; PDBConstruct 1–451; UniProt 1–451 Author chain 3F; PDBConstruct 1–451; UniProt 1–451 Author chain 3G; PDBConstruct 1–451; UniProt 1–451 Author chain 3I; PDBConstruct 1–451; UniProt 1–451 Author chain 3J; PDBConstruct 1–451; UniProt 1–451 Author chain 3K; PDBConstruct 1–451; UniProt 1–451 Author chain 3L; PDBConstruct 1–451; UniProt 1–451 Author chain 3M; PDBConstruct 1–451; UniProt 1–451 Author chain 3N; PDBConstruct 1–451; UniProt 1–451 Author chain 4A; PDBConstruct 1–451; UniProt 1–451 Author chain 4B; PDBConstruct 1–451; UniProt 1–451 Author chain 4C; PDBConstruct 1–451; UniProt 1–451 Author chain 4D; PDBConstruct 1–451; UniProt 1–451 Author chain 4E; PDBConstruct 1–451; UniProt 1–451 Author chain 4F; PDBConstruct 1–451; UniProt 1–451 Author chain 4G; PDBConstruct 1–451; UniProt 1–451 Author chain 4I; PDBConstruct 1–451; UniProt 1–451 Author chain 4J; PDBConstruct 1–451; UniProt 1–451 Author chain 4K; PDBConstruct 1–451; UniProt 1–451 Author chain 4L; PDBConstruct 1–451; UniProt 1–451 Author chain 4M; PDBConstruct 1–451; UniProt 1–451 Author chain 4N; PDBConstruct 1–451; UniProt 1–451

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 × 104 PDB declaration: 104-meric(104) Consistent with protein copy count Chain 1H; UniProt 1–445 Chain 1O; UniProt 1–445 Chain 1P; UniProt 1–445 Chain 1Q; UniProt 1–445 Chain 1R; UniProt 1–445 Chain 1S; UniProt 1–445 Chain 1T; UniProt 1–445 Chain 1U; UniProt 1–445 Chain 1V; UniProt 1–445 Chain 1W; UniProt 1–445 Chain 1X; UniProt 1–445 Chain 1Y; UniProt 1–445 Chain 1Z; UniProt 1–445 Chain 2H; UniProt 1–445 Chain 2O; UniProt 1–445 Chain 2P; UniProt 1–445 Chain 2Q; UniProt 1–445 Chain 2R; UniProt 1–445 Chain 2S; UniProt 1–445 Chain 2T; UniProt 1–445 Chain 2U; UniProt 1–445 Chain 2V; UniProt 1–445 Chain 2W; UniProt 1–445 Chain 2X; UniProt 1–445 Chain 2Y; UniProt 1–445 Chain 2Z; UniProt 1–445 Chain 3H; UniProt 1–445 Chain 3O; UniProt 1–445 Chain 3P; UniProt 1–445 Chain 3Q; UniProt 1–445 Chain 3R; UniProt 1–445 Chain 3S; UniProt 1–445 Chain 3T; UniProt 1–445 Chain 3U; UniProt 1–445 Chain 3V; UniProt 1–445 Chain 3W; UniProt 1–445 Chain 3X; UniProt 1–445 Chain 3Y; UniProt 1–445 Chain 3Z; UniProt 1–445 Chain 4H; UniProt 1–445 Chain 4O; UniProt 1–445 Chain 4P; UniProt 1–445 Chain 4Q; UniProt 1–445 Chain 4R; UniProt 1–445 Chain 4S; UniProt 1–445 Chain 4T; UniProt 1–445 Chain 4U; UniProt 1–445 Chain 4V; UniProt 1–445 Chain 4W; UniProt 1–445 Chain 4X; UniProt 1–445 Chain 4Y; UniProt 1–445 Chain 4Z; UniProt 1–445 Not recorded Tubulin alpha-1B chain × 52 (Q2XVP4) GTP GUANOSINE-5'-TRIPHOSPHATE × 52 MG MAGNESIUM ION × 52 GDP GUANOSINE-5'-DIPHOSPHATE × 52 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8;Contains 80 mM PIPES, 1 mM MgCl2, 1 mM EGTA, pH 6.8 with KOH (stored at 4 degrees Celsius). cryo-EM vitrification conditions:Cryogen ETHANE;Blotted for 4 seconds at blot force 10. Resolution 4.10 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 1H; PDBConstruct 1–445; UniProt 1–445 Author chain 1O; PDBConstruct 1–445; UniProt 1–445 Author chain 1P; PDBConstruct 1–445; UniProt 1–445 Author chain 1Q; PDBConstruct 1–445; UniProt 1–445 Author chain 1R; PDBConstruct 1–445; UniProt 1–445 Author chain 1S; PDBConstruct 1–445; UniProt 1–445 Author chain 1T; PDBConstruct 1–445; UniProt 1–445 Author chain 1U; PDBConstruct 1–445; UniProt 1–445 Author chain 1V; PDBConstruct 1–445; UniProt 1–445 Author chain 1W; PDBConstruct 1–445; UniProt 1–445 Author chain 1X; PDBConstruct 1–445; UniProt 1–445 Author chain 1Y; PDBConstruct 1–445; UniProt 1–445 Author chain 1Z; PDBConstruct 1–445; UniProt 1–445 Author chain 2H; PDBConstruct 1–445; UniProt 1–445 Author chain 2O; PDBConstruct 1–445; UniProt 1–445 Author chain 2P; PDBConstruct 1–445; UniProt 1–445 Author chain 2Q; PDBConstruct 1–445; UniProt 1–445 Author chain 2R; PDBConstruct 1–445; UniProt 1–445 Author chain 2S; PDBConstruct 1–445; UniProt 1–445 Author chain 2T; PDBConstruct 1–445; UniProt 1–445 Author chain 2U; PDBConstruct 1–445; UniProt 1–445 Author chain 2V; PDBConstruct 1–445; UniProt 1–445 Author chain 2W; PDBConstruct 1–445; UniProt 1–445 Author chain 2X; PDBConstruct 1–445; UniProt 1–445 Author chain 2Y; PDBConstruct 1–445; UniProt 1–445 Author chain 2Z; PDBConstruct 1–445; UniProt 1–445 Author chain 3H; PDBConstruct 1–445; UniProt 1–445 Author chain 3O; PDBConstruct 1–445; UniProt 1–445 Author chain 3P; PDBConstruct 1–445; UniProt 1–445 Author chain 3Q; PDBConstruct 1–445; UniProt 1–445 Author chain 3R; PDBConstruct 1–445; UniProt 1–445 Author chain 3S; PDBConstruct 1–445; UniProt 1–445 Author chain 3T; PDBConstruct 1–445; UniProt 1–445 Author chain 3U; PDBConstruct 1–445; UniProt 1–445 Author chain 3V; PDBConstruct 1–445; UniProt 1–445 Author chain 3W; PDBConstruct 1–445; UniProt 1–445 Author chain 3X; PDBConstruct 1–445; UniProt 1–445 Author chain 3Y; PDBConstruct 1–445; UniProt 1–445 Author chain 3Z; PDBConstruct 1–445; UniProt 1–445 Author chain 4H; PDBConstruct 1–445; UniProt 1–445 Author chain 4O; PDBConstruct 1–445; UniProt 1–445 Author chain 4P; PDBConstruct 1–445; UniProt 1–445 Author chain 4Q; PDBConstruct 1–445; UniProt 1–445 Author chain 4R; PDBConstruct 1–445; UniProt 1–445 Author chain 4S; PDBConstruct 1–445; UniProt 1–445 Author chain 4T; PDBConstruct 1–445; UniProt 1–445 Author chain 4U; PDBConstruct 1–445; UniProt 1–445 Author chain 4V; PDBConstruct 1–445; UniProt 1–445 Author chain 4W; PDBConstruct 1–445; UniProt 1–445 Author chain 4X; PDBConstruct 1–445; UniProt 1–445 Author chain 4Y; PDBConstruct 1–445; UniProt 1–445 Author chain 4Z; 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 6o2t

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6o2t
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6o2t
Deposition date deposition_date2019-02-24
Structure title titleAcetylated Microtubules
Keywords keywordsmicrotubule, cytoskeleton, acetylation, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron148.40
Forward intensity I(0) i0370320000000.00
Molecular weight molecular_weight5070500.0 kDa
Excluded volume excluded_volume6275000 ų
Envelope volume envelope_volume13069000 ų
Hydration-shell volume shell_volume748070 ų
Envelope diameter envelope_diameter477.7
Shell Rg shell_rg153.90
Envelope Rg envelope_rg132.20
Shape Rg shape_rg148.40
Total Rg total_rg148.40
Total atoms total_atoms355888
Residues n_residues45032
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 dmax397.5
Rg (real space) rg_real145.60
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real3.5580e+11
I(0) uncertainty (real space) i0_real_error8.2660e+09
Rg (reciprocal space) rg_reciprocal168.70
I(0) (reciprocal space) i0_reciprocal408300000000.0000
Solution quality estimate total_estimate0.8085
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary198.7
Skewness Skewness skewness-0.114
Kurtosis Kurtosis kurtosis-0.368
Angular range angular_range— – 0.0500 −1
Current regularization parameter α current_alpha1.4530
Highest regularization parameter α highest_alpha21200000000.0000
Real-space data points n_real_points11
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.838; Stabil: 0.952; Sysdev: 1.000; Positv: 1.000; Valcen: 0.181; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)