7pqc

tau-microtubule structural ensemble based on CryoEM data

Method: ELECTRON MICROSCOPY Dmax: 324.1 Å Quality: REASONABLE

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

Tubulin beta chain

Sus scrofa

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain A; UniProt 1–445 Chain C; UniProt 1–445 Chain E; UniProt 1–445 Chain G; UniProt 1–445 Chain I; UniProt 1–445 Chain K; UniProt 1–445 Chain M; UniProt 1–445 Not recorded Tubulin alpha-1B chain × 7 (Q2XVP4) Isoform Tau-F of Microtubule-associated protein tau × 1 (P10636) GDP GUANOSINE-5'-DIPHOSPHATE × 7 GTP GUANOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–445; UniProt 1–445 Author chain C; PDBConstruct 1–445; UniProt 1–445 Author chain E; PDBConstruct 1–445; UniProt 1–445 Author chain G; PDBConstruct 1–445; UniProt 1–445 Author chain I; PDBConstruct 1–445; UniProt 1–445 Author chain K; PDBConstruct 1–445; UniProt 1–445 Author chain M; PDBConstruct 1–445; UniProt 1–445

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain B; UniProt 1–451 Chain D; UniProt 1–451 Chain F; UniProt 1–451 Chain H; UniProt 1–451 Chain J; UniProt 1–451 Chain L; UniProt 1–451 Chain N; UniProt 1–451 Not recorded Tubulin beta chain × 7 (P02554) Isoform Tau-F of Microtubule-associated protein tau × 1 (P10636) GDP GUANOSINE-5'-DIPHOSPHATE × 7 GTP GUANOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–451; UniProt 1–451 Author chain D; PDBConstruct 1–451; UniProt 1–451 Author chain F; PDBConstruct 1–451; UniProt 1–451 Author chain H; PDBConstruct 1–451; UniProt 1–451 Author chain J; PDBConstruct 1–451; UniProt 1–451 Author chain L; PDBConstruct 1–451; UniProt 1–451 Author chain N; PDBConstruct 1–451; UniProt 1–451

Isoform Tau-F of Microtubule-associated protein tau

Homo sapiens

UniProt P10636

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 × 15 PDB declaration: pentadecameric(15) Consistent with protein copy count Chain O; UniProt 202–395 Not recorded Tubulin beta chain × 7 (P02554) Tubulin alpha-1B chain × 7 (Q2XVP4) GDP GUANOSINE-5'-DIPHOSPHATE × 7 GTP GUANOSINE-5'-TRIPHOSPHATE × 7 MG MAGNESIUM ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 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.

248 other PDB entries and 270 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TAU_HUMAN
Isoform P10636-8
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 1–194; UniProt 202–395

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 7pqc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7pqc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7pqc
Deposition date deposition_date2021-09-16
Structure title titletau-microtubule structural ensemble based on CryoEM data
Keywords keywordsComplex, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron163.30
Forward intensity I(0) i07832080000.00
Molecular weight molecular_weight727280.0 kDa
Excluded volume excluded_volume898520 ų
Envelope volume envelope_volume1546000 ų
Hydration-shell volume shell_volume107370 ų
Envelope diameter envelope_diameter585.4
Shell Rg shell_rg63.07
Envelope Rg envelope_rg168.10
Shape Rg shape_rg163.30
Total Rg total_rg162.50
Total atoms total_atoms51036
Residues n_residues6466
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 dmax324.1
Rg (real space) rg_real112.70
Rg uncertainty (real space) rg_real_error1.45
I(0) (real space) i0_real6.4040e+09
I(0) uncertainty (real space) i0_real_error1.3800e+08
Rg (reciprocal space) rg_reciprocal101.40
I(0) (reciprocal space) i0_reciprocal6611000000.0000
Solution quality estimate total_estimate0.6881
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.0
Skewness Skewness skewness0.297
Kurtosis Kurtosis kurtosis-1.100
Angular range angular_range— – 0.0450 −1
Current regularization parameter α current_alpha2.8720
Highest regularization parameter α highest_alpha99610000.0000
Real-space data points n_real_points10
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.379; Oscil: 0.574; Stabil: 0.785; Sysdev: 1.000; Positv: 1.000; Valcen: 0.867; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)