6lsn

Crystal structure of tubulin-inhibitor complex

Method: X-RAY DIFFRACTION Dmax: 182.8 Å Quality: REASONABLE

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

Tubulin alpha-1B chain

Sus scrofa

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 (A0A287AGU7) Stathmin-4 × 1 (P63042) Tubulin tyrosine ligase × 1 (E1BQ43) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 CA CALCIUM ION × 4 CL CHLORIDE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 ERR 2-(1-methylindol-5-yl)-7-(3,4,5-trimethoxyphenyl)pyrazolo[1,5-a]pyrimidine × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.7;277 K;6% PEG, 5% glycerol, 0.1M MES, 30 mM CaCl2, 30 mM MgCl2, pH 6.7 Resolution 2.44 Å R-free 0.220

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

Sus scrofa

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–445 Chain D; UniProt 1–445 Not recorded Tubulin alpha-1B chain × 2 (Q2XVP4) Stathmin-4 × 1 (P63042) Tubulin tyrosine ligase × 1 (E1BQ43) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 CA CALCIUM ION × 4 CL CHLORIDE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 ERR 2-(1-methylindol-5-yl)-7-(3,4,5-trimethoxyphenyl)pyrazolo[1,5-a]pyrimidine × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.7;277 K;6% PEG, 5% glycerol, 0.1M MES, 30 mM CaCl2, 30 mM MgCl2, pH 6.7 Resolution 2.44 Å R-free 0.220

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 1–445; UniProt 1–445 Author chain D; PDBConstruct 1–445; UniProt 1–445

Stathmin-4

Mus musculus

UniProt P63042

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 Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (A0A287AGU7) Tubulin tyrosine ligase × 1 (E1BQ43) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 CA CALCIUM ION × 4 CL CHLORIDE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 ERR 2-(1-methylindol-5-yl)-7-(3,4,5-trimethoxyphenyl)pyrazolo[1,5-a]pyrimidine × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.7;277 K;6% PEG, 5% glycerol, 0.1M MES, 30 mM CaCl2, 30 mM MgCl2, pH 6.7 Resolution 2.44 Å R-free 0.220

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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STMN4_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 3–143; UniProt 49–189

Tubulin tyrosine ligase

Gallus gallus

UniProt E1BQ43

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 Tubulin alpha-1B chain × 2 (Q2XVP4) Tubulin beta chain × 2 (A0A287AGU7) Stathmin-4 × 1 (P63042) GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 6 CA CALCIUM ION × 4 CL CHLORIDE ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 2 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 ERR 2-(1-methylindol-5-yl)-7-(3,4,5-trimethoxyphenyl)pyrazolo[1,5-a]pyrimidine × 1 ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.7;277 K;6% PEG, 5% glycerol, 0.1M MES, 30 mM CaCl2, 30 mM MgCl2, pH 6.7 Resolution 2.44 Å R-free 0.220

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.

241 other PDB entries and 241 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E1BQ43_CHICK
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 6lsn

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6lsn
Deposition date deposition_date2020-01-17
Structure title titleCrystal structure of tubulin-inhibitor complex
Keywords keywordsInhibitor, 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_guinier56.26
Radius of gyration Rg (electron density) rg_electron57.11
Forward intensity I(0) i0951065000.00
Molecular weight molecular_weight251150.0 kDa
Excluded volume excluded_volume311480 ų
Envelope volume envelope_volume421840 ų
Hydration-shell volume shell_volume67138 ų
Envelope diameter envelope_diameter202.4
Shell Rg shell_rg50.93
Envelope Rg envelope_rg57.35
Shape Rg shape_rg57.12
Total Rg total_rg56.88
Total atoms total_atoms17618
Residues n_residues2200
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 dmax182.8
Rg (real space) rg_real57.01
Rg uncertainty (real space) rg_real_error2.36
I(0) (real space) i0_real9.5110e+08
I(0) uncertainty (real space) i0_real_error2.0400e+07
Rg (reciprocal space) rg_reciprocal55.60
I(0) (reciprocal space) i0_reciprocal949000000.0000
Solution quality estimate total_estimate0.7147
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.2
Skewness Skewness skewness0.553
Kurtosis Kurtosis kurtosis-0.567
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha88370000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.562; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.602; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (13)

7. Fold Classification (SCOP + CATH) 14 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd6lsna1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6lsna2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6lsnb1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6lsnb2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6lsnc1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6lsnc2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6lsnd1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.32 — Tubulin nucleotide-binding domain-like
Superfamily Superfamily superfamilyc.32.1 — Tubulin nucleotide-binding domain-like
Family Family familyc.32.1.1 — Tubulin, GTPase domain
Domain ID domain_idd6lsnd2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.79 — Bacillus chorismate mutase-like
Superfamily Superfamily superfamilyd.79.2 — Tubulin C-terminal domain-like
Family Family familyd.79.2.1 — Tubulin, C-terminal domain
Domain ID domain_idd6lsne_
Class classa — All alpha proteins
Fold Fold folda.137 — Non-globular all-alpha subunits of globular proteins
Superfamily Superfamily superfamilya.137.10 — Stathmin
Family Family familya.137.10.1 — Stathmin
Domain ID domain_idd6lsnf1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.30 — PreATP-grasp domain
Superfamily Superfamily superfamilyc.30.1 — PreATP-grasp domain
Family Family familyc.30.1.9 — Tubulin tyrosine ligase (TTL) N-terminal domain-like
Domain ID domain_idd6lsnf2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.142 — ATP-grasp
Superfamily Superfamily superfamilyd.142.1 — Glutathione synthetase ATP-binding domain-like
Family Family familyd.142.1.10 — Tubulin tyrosine ligase (TTL) C-terminal domain-like
Domain ID domain_idd6lsnf3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id6lsnF01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily11480
Domain ID domain_id6lsnF02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily20 — ATP-grasp fold, B domain

8. Citations (1)

9. Files and Curves (10)