9kbn

Crystal structure of T2R-TTL-IKP104-Colchicine

Method: X-RAY DIFFRACTION Dmax: 184.5 Å Quality: SUSPICIOUS

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

Detyrosinated 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–450 Chain C; UniProt 1–450 Not recorded Tubulin beta chain × 2 (A0A8D0VN39) Stathmin-4 × 1 (P63043) Tubulin tyrosine ligase × 1 (A0A8V0Z8P0) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 CA CALCIUM ION × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 W4Q 1-(2-chloranyl-3,5-dimethoxy-phenyl)-2-(4-fluorophenyl)-3-methyl-6-phenyl-pyridin-4-one × 1 LOC N-[(7S)-1,2,3,10-tetramethoxy-9-oxo-6,7-dihydro-5H-benzo[d]heptalen-7-yl]ethanamide × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;6% poly(ethylene glycol) 4000, 8% glycerol, 0.1 M MES (pH 6.7), 30 mM CaCl2 and 30 mM MgCl2. Resolution 2.56 Å R-free 0.262

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 1–450; UniProt 1–450 Author chain C; PDBConstruct 1–450; UniProt 1–450

Tubulin beta chain

OrganismNot specified

UniProt A0A8D0VN39

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–431 Chain D; UniProt 1–431 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (Q2XVP4) Stathmin-4 × 1 (P63043) Tubulin tyrosine ligase × 1 (A0A8V0Z8P0) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 CA CALCIUM ION × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 W4Q 1-(2-chloranyl-3,5-dimethoxy-phenyl)-2-(4-fluorophenyl)-3-methyl-6-phenyl-pyridin-4-one × 1 LOC N-[(7S)-1,2,3,10-tetramethoxy-9-oxo-6,7-dihydro-5H-benzo[d]heptalen-7-yl]ethanamide × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;6% poly(ethylene glycol) 4000, 8% glycerol, 0.1 M MES (pH 6.7), 30 mM CaCl2 and 30 mM MgCl2. Resolution 2.56 Å R-free 0.262

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8D0VN39_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–431; UniProt 1–431 Author chain D; PDBConstruct 1–431; UniProt 1–431

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 49–189 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (A0A8D0VN39) Tubulin tyrosine ligase × 1 (A0A8V0Z8P0) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 CA CALCIUM ION × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 W4Q 1-(2-chloranyl-3,5-dimethoxy-phenyl)-2-(4-fluorophenyl)-3-methyl-6-phenyl-pyridin-4-one × 1 LOC N-[(7S)-1,2,3,10-tetramethoxy-9-oxo-6,7-dihydro-5H-benzo[d]heptalen-7-yl]ethanamide × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;6% poly(ethylene glycol) 4000, 8% glycerol, 0.1 M MES (pH 6.7), 30 mM CaCl2 and 30 mM MgCl2. Resolution 2.56 Å R-free 0.262

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

Tubulin tyrosine ligase

Gallus gallus

UniProt A0A8V0Z8P0

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain F; UniProt 1–411 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (A0A8D0VN39) Stathmin-4 × 1 (P63043) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 5 CA CALCIUM ION × 7 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 W4Q 1-(2-chloranyl-3,5-dimethoxy-phenyl)-2-(4-fluorophenyl)-3-methyl-6-phenyl-pyridin-4-one × 1 LOC N-[(7S)-1,2,3,10-tetramethoxy-9-oxo-6,7-dihydro-5H-benzo[d]heptalen-7-yl]ethanamide × 2 GDP GUANOSINE-5'-DIPHOSPHATE × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;298 K;6% poly(ethylene glycol) 4000, 8% glycerol, 0.1 M MES (pH 6.7), 30 mM CaCl2 and 30 mM MgCl2. Resolution 2.56 Å R-free 0.262

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.

25 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8V0Z8P0_CHICK
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–378; UniProt 1–411

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 9kbn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9kbn
Deposition date deposition_date2024-10-31
最后修订 last_revision2025-11-05
Structure title titleCrystal structure of T2R-TTL-IKP104-Colchicine
Keywords keywordsMicrotubule, Cell Cycle; CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier55.68
Radius of gyration Rg (electron density) rg_electron56.32
Forward intensity I(0) i0916631000.00
Molecular weight molecular_weight244550.0 kDa
Excluded volume excluded_volume301840 ų
Envelope volume envelope_volume404730 ų
Hydration-shell volume shell_volume65720 ų
Envelope diameter envelope_diameter204.7
Shell Rg shell_rg50.09
Envelope Rg envelope_rg56.52
Shape Rg shape_rg56.23
Total Rg total_rg56.44
Total atoms total_atoms33275
Residues n_residues2196
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 dmax184.5
Rg (real space) rg_real56.41
Rg uncertainty (real space) rg_real_error2.10
I(0) (real space) i0_real9.1660e+08
I(0) uncertainty (real space) i0_real_error1.8600e+07
Rg (reciprocal space) rg_reciprocal55.03
I(0) (reciprocal space) i0_reciprocal914700000.0000
Solution quality estimate total_estimate0.4990
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.5
Skewness Skewness skewness0.560
Kurtosis Kurtosis kurtosis-0.547
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha85610000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.591; Stabil: 0.999; Sysdev: 0.041; Positv: 1.000; Valcen: 0.574; Smooth: 0.014

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

8. Citations (1)

9. Files and Curves (10)