9o6i

TUBULIN-RB3_SLD IN COMPLEX WITH COMPOUND QW-5-70

Method: X-RAY DIFFRACTION Dmax: 174.7 Å Quality: SUSPICIOUS

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–438 Chain C; UniProt 1–438 Not recorded Tubulin beta chain × 2 (A0A287AGU7) Stathmin-4 × 1 (P63043) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 A1B97 [(4M)-4-(1H-indazol-4-yl)-1H-imidazol-2-yl](3,4,5-trimethoxyphenyl)methanone × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;293.15 K;0.1 M trisodium citrate, pH 5.6, 0.2 M ammonium sulfate, 12.2% PEG 4000 Resolution 2.51 Å R-free 0.244

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 A; PDBConstruct 1–438; UniProt 1–438 Author chain C; PDBConstruct 1–438; UniProt 1–438

Tubulin beta chain

OrganismNot specified

UniProt A0A287AGU7

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–433 Chain D; UniProt 1–433 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Stathmin-4 × 1 (P63043) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 A1B97 [(4M)-4-(1H-indazol-4-yl)-1H-imidazol-2-yl](3,4,5-trimethoxyphenyl)methanone × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;293.15 K;0.1 M trisodium citrate, pH 5.6, 0.2 M ammonium sulfate, 12.2% PEG 4000 Resolution 2.51 Å R-free 0.244

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.

98 other PDB entries and 98 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A287AGU7_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–433; UniProt 1–433 Author chain D; PDBConstruct 1–433; UniProt 1–433

Stathmin-4

Rattus norvegicus

UniProt P63043

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain E; UniProt 49–189 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (A0A287AGU7) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 2 A1B97 [(4M)-4-(1H-indazol-4-yl)-1H-imidazol-2-yl](3,4,5-trimethoxyphenyl)methanone × 2 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;293.15 K;0.1 M trisodium citrate, pH 5.6, 0.2 M ammonium sulfate, 12.2% PEG 4000 Resolution 2.51 Å R-free 0.244

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.

287 other PDB entries and 287 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STMN4_RAT
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 3–143; UniProt 49–189

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 9o6i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o6i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9o6i
Deposition date deposition_date2025-04-13
最后修订 last_revision2026-04-08
Structure title titleTUBULIN-RB3_SLD IN COMPLEX WITH COMPOUND QW-5-70
Keywords keywordsMICROTUBULE INHIBITOR, COLCHICINE, CELL CYCLE, CANCER, CELL CYCLE INHIBITOR COMPLEX; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier51.30
Radius of gyration Rg (electron density) rg_electron52.14
Forward intensity I(0) i01252090000.00
Molecular weight molecular_weight191700.0 kDa
Excluded volume excluded_volume183570 ų
Envelope volume envelope_volume325690 ų
Hydration-shell volume shell_volume58446 ų
Envelope diameter envelope_diameter183.2
Shell Rg shell_rg46.63
Envelope Rg envelope_rg52.53
Shape Rg shape_rg52.13
Total Rg total_rg52.01
Total atoms total_atoms14430
Residues n_residues1833
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 dmax174.7
Rg (real space) rg_real52.02
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real1.2520e+09
I(0) uncertainty (real space) i0_real_error2.6320e+07
Rg (reciprocal space) rg_reciprocal50.70
I(0) (reciprocal space) i0_reciprocal1250000000.0000
Solution quality estimate total_estimate0.4393
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.8
Skewness Skewness skewness0.663
Kurtosis Kurtosis kurtosis-0.377
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha139900000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.410; Stabil: 0.999; Sysdev: 0.029; Positv: 1.000; Valcen: 0.296; Smooth: 0.098

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)