9f3r

13pf E254Q microtubule from recombinant human tubulin decorated with EB3

Method: ELECTRON MICROSCOPY Dmax: 227.6 Å Quality: GOOD

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

Microtubule-associated protein RP/EB family member 3

Homo sapiens

UniProt Q9UPY8

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain S; UniProt 1–131 Chain T; UniProt 1–131 Not recorded Detyrosinated tubulin alpha-1B chain × 6 (P68363) 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MARE3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain S; PDBConstruct 1–131; UniProt 1–131 Author chain T; PDBConstruct 1–131; UniProt 1–131

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 × 14 PDB declaration: 14-meric(14) Consistent with protein copy count Chain A; UniProt 1–42 Chain A; UniProt 47–441 Chain C; UniProt 1–42 Chain C; UniProt 47–441 Chain E; UniProt 1–42 Chain E; UniProt 47–441 Chain G; UniProt 1–42 Chain G; UniProt 47–441 Chain I; UniProt 1–42 Chain I; UniProt 47–441 Chain K; UniProt 1–42 Chain K; UniProt 47–441 Not recorded Microtubule-associated protein RP/EB family member 3 × 2 (Q9UPY8) 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 2
Chains and sequence ranges Author chain A; PDBConstruct 1–42; UniProt 1–42 Author chain A; PDBConstruct 59–453; UniProt 47–441 Author chain C; PDBConstruct 1–42; UniProt 1–42 Author chain C; PDBConstruct 59–453; UniProt 47–441 Author chain E; PDBConstruct 1–42; UniProt 1–42 Author chain E; PDBConstruct 59–453; UniProt 47–441 Author chain G; PDBConstruct 1–42; UniProt 1–42 Author chain G; PDBConstruct 59–453; UniProt 47–441 Author chain I; PDBConstruct 1–42; UniProt 1–42 Author chain I; PDBConstruct 59–453; UniProt 47–441 Author chain K; PDBConstruct 1–42; UniProt 1–42 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 × 14 PDB declaration: 14-meric(14) 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 Microtubule-associated protein RP/EB family member 3 × 2 (Q9UPY8) 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 3
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 9f3r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9f3r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9f3r
Deposition date deposition_date2024-04-25
最后修订 last_revision2025-03-19
Structure title title13pf E254Q microtubule from recombinant human tubulin decorated with EB3
Keywords keywordsMicrotubule Tubulin GTP cp 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_guinier66.38
Radius of gyration Rg (electron density) rg_electron66.32
Forward intensity I(0) i05586200000.00
Molecular weight molecular_weight616420.0 kDa
Excluded volume excluded_volume763880 ų
Envelope volume envelope_volume1092200 ų
Hydration-shell volume shell_volume136100 ų
Envelope diameter envelope_diameter242.7
Shell Rg shell_rg66.59
Envelope Rg envelope_rg65.15
Shape Rg shape_rg66.32
Total Rg total_rg66.31
Total atoms total_atoms43264
Residues n_residues5446
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 dmax227.6
Rg (real space) rg_real66.42
Rg uncertainty (real space) rg_real_error2.54
I(0) (real space) i0_real5.5860e+09
I(0) uncertainty (real space) i0_real_error1.2060e+08
Rg (reciprocal space) rg_reciprocal66.29
I(0) (reciprocal space) i0_reciprocal5585000000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.9
Skewness Skewness skewness0.289
Kurtosis Kurtosis kurtosis-0.438
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha230700000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.777

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)