3j7i

Structure of alpha- and beta- tubulin in GMPCPP-microtubules

Method: ELECTRON MICROSCOPY Dmax: 100.4 Å Quality: REASONABLE

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

Tubulin alpha-1A chain

OrganismNot specified

UniProt P02550

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–451 Not recorded Tubulin beta chain × 1 (P02554) MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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.

39 other PDB entries and 46 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TBA1A_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–451; UniProt 1–451

Tubulin beta chain

OrganismNot specified

UniProt P02554

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–445 Not recorded Tubulin alpha-1A chain × 1 (P02550) MG MAGNESIUM ION × 2 GTP GUANOSINE-5'-TRIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.90 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.

137 other PDB entries and 159 assemblies. Open the comparison page and filter oligomeric states

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

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 3j7i

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j7i
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j7i
Deposition date deposition_date2014-07-01
Structure title titleStructure of alpha- and beta- tubulin in GMPCPP-microtubules
Keywords keywordsMicrotubule, Tubulin, GTP-state structure, GMPCPP, Microtubule stabilaization, Micotubule polymerization, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.82
Radius of gyration Rg (electron density) rg_electron29.20
Forward intensity I(0) i0144507000.00
Molecular weight molecular_weight92851.0 kDa
Excluded volume excluded_volume114960 ų
Envelope volume envelope_volume137760 ų
Hydration-shell volume shell_volume39118 ų
Envelope diameter envelope_diameter107.3
Shell Rg shell_rg36.67
Envelope Rg envelope_rg29.39
Shape Rg shape_rg29.21
Total Rg total_rg29.80
Total atoms total_atoms6515
Residues n_residues820
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 dmax100.4
Rg (real space) rg_real29.86
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real1.4450e+08
I(0) uncertainty (real space) i0_real_error2.2130e+06
Rg (reciprocal space) rg_reciprocal29.84
I(0) (reciprocal space) i0_reciprocal144500000.0000
Solution quality estimate total_estimate0.6740
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.2
Skewness Skewness skewness0.430
Kurtosis Kurtosis kurtosis-0.250
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha30620000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 0.135; Positv: 1.000; Valcen: 0.988; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (2)

9. Files and Curves (10)