8wmo

Crystal structure analysis of tubulin and heterocyclic podophyllotoxins complex for anticancer agents

Method: X-RAY DIFFRACTION Dmax: 180.5 Å Quality: REASONABLE

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 1–440 Chain C; UniProt 1–440 Not recorded Tubulin beta chain × 2 (A0A8D1UIR5) Stathmin-4 × 1 (P63043) Tubulin--tyrosine ligase × 1 (A0A8C9FGJ1) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 EDO 1,2-ETHANEDIOL × 8 PEG DI(HYDROXYETHYL)ETHER × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 WIW (5~{S},5~{a}~{R},8~{a}~{R},9~{R})-5-pyrimidin-2-ylsulfanyl-9-(3,4,5-trimethoxyphenyl)-5~{a},6,8~{a},9-tetrahydro-5~{H}-[2]benzofuro[5,6-f][1,3]benzodioxol-8-one × 1 CA CALCIUM ION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;6% glycerol, 6% PEG4000, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES-Na Resolution 2.89 Å R-free 0.266

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 1–440; UniProt 1–440 Author chain C; PDBConstruct 1–440; UniProt 1–440

Tubulin beta chain

OrganismNot specified

UniProt A0A8D1UIR5

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 1–445 Chain D; UniProt 1–445 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (Q2XVP4) Stathmin-4 × 1 (P63043) Tubulin--tyrosine ligase × 1 (A0A8C9FGJ1) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 EDO 1,2-ETHANEDIOL × 8 PEG DI(HYDROXYETHYL)ETHER × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 WIW (5~{S},5~{a}~{R},8~{a}~{R},9~{R})-5-pyrimidin-2-ylsulfanyl-9-(3,4,5-trimethoxyphenyl)-5~{a},6,8~{a},9-tetrahydro-5~{H}-[2]benzofuro[5,6-f][1,3]benzodioxol-8-one × 1 CA CALCIUM ION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;6% glycerol, 6% PEG4000, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES-Na Resolution 2.89 Å R-free 0.266

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8D1UIR5_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 1–445 Author chain D; PDBConstruct 1–445; UniProt 1–445

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 50–187 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (A0A8D1UIR5) Tubulin--tyrosine ligase × 1 (A0A8C9FGJ1) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 EDO 1,2-ETHANEDIOL × 8 PEG DI(HYDROXYETHYL)ETHER × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 WIW (5~{S},5~{a}~{R},8~{a}~{R},9~{R})-5-pyrimidin-2-ylsulfanyl-9-(3,4,5-trimethoxyphenyl)-5~{a},6,8~{a},9-tetrahydro-5~{H}-[2]benzofuro[5,6-f][1,3]benzodioxol-8-one × 1 CA CALCIUM ION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;6% glycerol, 6% PEG4000, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES-Na Resolution 2.89 Å R-free 0.266

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 1–138; UniProt 50–187

Tubulin--tyrosine ligase

Gallus gallus

UniProt A0A8C9FGJ1

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 1–378 Not recorded Detyrosinated tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (A0A8D1UIR5) Stathmin-4 × 1 (P63043) GTP GUANOSINE-5'-TRIPHOSPHATE × 3 MG MAGNESIUM ION × 4 EDO 1,2-ETHANEDIOL × 8 PEG DI(HYDROXYETHYL)ETHER × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 WIW (5~{S},5~{a}~{R},8~{a}~{R},9~{R})-5-pyrimidin-2-ylsulfanyl-9-(3,4,5-trimethoxyphenyl)-5~{a},6,8~{a},9-tetrahydro-5~{H}-[2]benzofuro[5,6-f][1,3]benzodioxol-8-one × 1 CA CALCIUM ION × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;6% glycerol, 6% PEG4000, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES-Na Resolution 2.89 Å R-free 0.266

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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A8C9FGJ1_PAVCR
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–378; UniProt 1–378

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 8wmo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wmo
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8wmo
Deposition date deposition_date2023-10-04
最后修订 last_revision2024-10-09
Structure title titleCrystal structure analysis of tubulin and heterocyclic podophyllotoxins complex for anticancer agents
Keywords keywordstubulin, heterocyclic podophyllotoxins complex, anticancer agents, 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_guinier55.14
Radius of gyration Rg (electron density) rg_electron55.94
Forward intensity I(0) i0860234000.00
Molecular weight molecular_weight237450.0 kDa
Excluded volume excluded_volume293700 ų
Envelope volume envelope_volume389840 ų
Hydration-shell volume shell_volume64007 ų
Envelope diameter envelope_diameter194.6
Shell Rg shell_rg49.70
Envelope Rg envelope_rg56.07
Shape Rg shape_rg55.96
Total Rg total_rg55.69
Total atoms total_atoms16676
Residues n_residues2153
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 dmax180.5
Rg (real space) rg_real55.85
Rg uncertainty (real space) rg_real_error1.98
I(0) (real space) i0_real8.6020e+08
I(0) uncertainty (real space) i0_real_error1.5780e+07
Rg (reciprocal space) rg_reciprocal54.51
I(0) (reciprocal space) i0_reciprocal858500000.0000
Solution quality estimate total_estimate0.7300
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.4
Skewness Skewness skewness0.565
Kurtosis Kurtosis kurtosis-0.538
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha92760000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.608; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.650; Smooth: 0.014

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

8. Citations (1)

9. Files and Curves (10)