8vt7

Structure of the gamma tubulin ring complex nucleated microtubule protofilament.

Method: ELECTRON MICROSCOPY Dmax: 167.5 Å Quality: SUSPICIOUS

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

Tubulin beta-3 chain

Homo sapiens

UniProt Q13509

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–450 Chain F; UniProt 1–450 Not recorded Tubulin alpha-1B chain × 2 (P68363) GDP GUANOSINE-5'-DIPHOSPHATE × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.66 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBB3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–450; UniProt 1–450 Author chain F; PDBConstruct 1–450; UniProt 1–450

Tubulin alpha-1B chain

Homo sapiens

UniProt P68363

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–451 Chain J; UniProt 1–451 Not recorded Tubulin beta-3 chain × 2 (Q13509) GDP GUANOSINE-5'-DIPHOSPHATE × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.66 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.

38 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1B_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–457; UniProt 1–451 Author chain J; PDBConstruct 1–457; UniProt 1–451

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 8vt7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8vt7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8vt7
Deposition date deposition_date2024-01-25
Structure title titleStructure of the gamma tubulin ring complex nucleated microtubule protofilament.
Keywords keywordsMicrotubule, CELL CYCLE; CELL CYCLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier48.24
Radius of gyration Rg (electron density) rg_electron49.47
Forward intensity I(0) i0578038000.00
Molecular weight molecular_weight193600.0 kDa
Excluded volume excluded_volume239810 ų
Envelope volume envelope_volume297140 ų
Hydration-shell volume shell_volume55793 ų
Envelope diameter envelope_diameter184.2
Shell Rg shell_rg45.41
Envelope Rg envelope_rg50.16
Shape Rg shape_rg49.48
Total Rg total_rg49.29
Total atoms total_atoms13590
Residues n_residues1722
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 dmax167.5
Rg (real space) rg_real49.34
Rg uncertainty (real space) rg_real_error1.84
I(0) (real space) i0_real5.7800e+08
I(0) uncertainty (real space) i0_real_error1.2050e+07
Rg (reciprocal space) rg_reciprocal48.25
I(0) (reciprocal space) i0_reciprocal577200000.0000
Solution quality estimate total_estimate0.4535
Solution quality rating solution_quality SUSPICIOUS a SUSPICIOUS solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.5
Skewness Skewness skewness0.674
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha196800000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.409; Stabil: 0.998; Sysdev: 0.006; Positv: 1.000; Valcen: 0.486; Smooth: 0.164

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)