3j6g

Minimized average structure of microtubules stabilized by taxol

Method: ELECTRON MICROSCOPY Dmax: 229.4 Å Quality: EXCELLENT

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

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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 1–439 Chain C; UniProt 1–439 Chain E; UniProt 1–439 Chain G; UniProt 1–439 Chain I; UniProt 1–439 Chain K; UniProt 1–439 Chain M; UniProt 1–439 Chain O; UniProt 1–439 Chain Q; UniProt 1–439 Not recorded Tubulin beta chain × 9 (P02554) GTP GUANOSINE-5'-TRIPHOSPHATE × 9 MG MAGNESIUM ION × 9 GDP GUANOSINE-5'-DIPHOSPHATE × 9 TA1 TAXOL × 9 ELECTRON MICROSCOPY cryo-EM buffer:80 mM PIPES, 1 mM EGTA, 1 mM MgCl2, 1 mM DTT, 0.05% Nonidet P-40;pH 6.8;80 mM PIPES, 1 mM EGTA, 1 mM MgCl2, 1 mM DTT, 0.05% Nonidet P-40 cryo-EM vitrification conditions:The grid was blotted for 2 seconds before plunging.;90.4 K;Cryogen ETHANE;The grid was blotted for 2 seconds before plunging into liquid ethane (FEI VITROBOT MARK II). Resolution 5.50 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.

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 Author chain C; PDBConstruct 1–439; UniProt 1–439 Author chain E; PDBConstruct 1–439; UniProt 1–439 Author chain G; PDBConstruct 1–439; UniProt 1–439 Author chain I; PDBConstruct 1–439; UniProt 1–439 Author chain K; PDBConstruct 1–439; UniProt 1–439 Author chain M; PDBConstruct 1–439; UniProt 1–439 Author chain O; PDBConstruct 1–439; UniProt 1–439 Author chain Q; 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 × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain B; UniProt 1–427 Chain D; UniProt 1–427 Chain F; UniProt 1–427 Chain H; UniProt 1–427 Chain J; UniProt 1–427 Chain L; UniProt 1–427 Chain N; UniProt 1–427 Chain P; UniProt 1–427 Chain R; UniProt 1–427 Not recorded Tubulin alpha-1A chain × 9 (P02550) GTP GUANOSINE-5'-TRIPHOSPHATE × 9 MG MAGNESIUM ION × 9 GDP GUANOSINE-5'-DIPHOSPHATE × 9 TA1 TAXOL × 9 ELECTRON MICROSCOPY cryo-EM buffer:80 mM PIPES, 1 mM EGTA, 1 mM MgCl2, 1 mM DTT, 0.05% Nonidet P-40;pH 6.8;80 mM PIPES, 1 mM EGTA, 1 mM MgCl2, 1 mM DTT, 0.05% Nonidet P-40 cryo-EM vitrification conditions:The grid was blotted for 2 seconds before plunging.;90.4 K;Cryogen ETHANE;The grid was blotted for 2 seconds before plunging into liquid ethane (FEI VITROBOT MARK II). Resolution 5.50 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–427; UniProt 1–427 Author chain D; PDBConstruct 1–427; UniProt 1–427 Author chain F; PDBConstruct 1–427; UniProt 1–427 Author chain H; PDBConstruct 1–427; UniProt 1–427 Author chain J; PDBConstruct 1–427; UniProt 1–427 Author chain L; PDBConstruct 1–427; UniProt 1–427 Author chain N; PDBConstruct 1–427; UniProt 1–427 Author chain P; PDBConstruct 1–427; UniProt 1–427 Author chain R; PDBConstruct 1–427; UniProt 1–427

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 3j6g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j6g
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j6g
Deposition date deposition_date2014-02-19
Structure title titleMinimized average structure of microtubules stabilized by taxol
Keywords keywordsmicrotubule, taxol, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier85.07
Radius of gyration Rg (electron density) rg_electron85.70
Forward intensity I(0) i011122100000.00
Molecular weight molecular_weight874950.0 kDa
Excluded volume excluded_volume1084100 ų
Envelope volume envelope_volume1521500 ų
Hydration-shell volume shell_volume153730 ų
Envelope diameter envelope_diameter310.8
Shell Rg shell_rg73.02
Envelope Rg envelope_rg84.20
Shape Rg shape_rg85.70
Total Rg total_rg85.55
Total atoms total_atoms61425
Residues n_residues7686
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 dmax229.4
Rg (real space) rg_real81.27
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real1.0660e+10
I(0) uncertainty (real space) i0_real_error2.2600e+08
Rg (reciprocal space) rg_reciprocal82.80
I(0) (reciprocal space) i0_reciprocal11050000000.0000
Solution quality estimate total_estimate0.9160
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary89.2
Skewness Skewness skewness0.291
Kurtosis Kurtosis kurtosis-0.643
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.9288
Highest regularization parameter α highest_alpha235700000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 1.000; Stabil: 0.978; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.007

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)