9f3h

Undecorated 13pf mosaic 20%E254Q - 80% E254QN microtubule from recombinant human tubulin

Method: ELECTRON MICROSCOPY Dmax: 230.7 Å Quality: GOOD

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

Detyrosinated 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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain A; UniProt 47–441 Chain C; UniProt 47–441 Chain E; UniProt 47–441 Chain G; UniProt 47–441 Chain I; UniProt 47–441 Chain K; UniProt 47–441 Not recorded Tubulin beta-3 chain × 6 (Q13509) GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 1
Chains and sequence ranges Author chain A; PDBConstruct 59–453; UniProt 47–441 Author chain C; PDBConstruct 59–453; UniProt 47–441 Author chain E; PDBConstruct 59–453; UniProt 47–441 Author chain G; PDBConstruct 59–453; UniProt 47–441 Author chain I; PDBConstruct 59–453; UniProt 47–441 Author chain K; PDBConstruct 59–453; UniProt 47–441

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain B; UniProt 1–450 Chain D; UniProt 1–450 Chain F; UniProt 1–450 Chain N; UniProt 1–450 Chain P; UniProt 1–450 Chain R; UniProt 1–450 Not recorded Detyrosinated tubulin alpha-1B chain × 6 (P68363) GTP GUANOSINE-5'-TRIPHOSPHATE × 12 MG MAGNESIUM ION × 12 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–450; UniProt 1–450 Author chain D; PDBConstruct 1–450; UniProt 1–450 Author chain F; PDBConstruct 1–450; UniProt 1–450 Author chain N; PDBConstruct 1–450; UniProt 1–450 Author chain P; PDBConstruct 1–450; UniProt 1–450 Author chain R; PDBConstruct 1–450; UniProt 1–450

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 9f3h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9f3h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9f3h
Deposition date deposition_date2024-04-25
最后修订 last_revision2025-03-19
Structure title titleUndecorated 13pf mosaic 20%E254Q - 80% E254QN microtubule from recombinant human tubulin
Keywords keywordsMicrotubule Tubulin GTP cap Cell cycle, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.29
Radius of gyration Rg (electron density) rg_electron67.29
Forward intensity I(0) i05079050000.00
Molecular weight molecular_weight585760.0 kDa
Excluded volume excluded_volume725000 ų
Envelope volume envelope_volume1043700 ų
Hydration-shell volume shell_volume128550 ų
Envelope diameter envelope_diameter241.6
Shell Rg shell_rg66.56
Envelope Rg envelope_rg65.90
Shape Rg shape_rg67.30
Total Rg total_rg67.25
Total atoms total_atoms41100
Residues n_residues5184
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 dmax230.7
Rg (real space) rg_real67.30
Rg uncertainty (real space) rg_real_error2.95
I(0) (real space) i0_real5.0790e+09
I(0) uncertainty (real space) i0_real_error1.1150e+08
Rg (reciprocal space) rg_reciprocal67.17
I(0) (reciprocal space) i0_reciprocal5077000000.0000
Solution quality estimate total_estimate0.8728
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary70.2
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.503
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha161700000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.870; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.738

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)