8fnz

Acetylated tau repeat 1 and 2 fragment (AcR1R2)

Method: ELECTRON MICROSCOPY Dmax: 124.1 Å Quality: REASONABLE

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

Microtubule-associated protein tau, acetylated repeat 1 and 2 fragment

OrganismNot specified

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 homooligomer Homooligomer Protein × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain A; UniProt 263–280 Chain B; UniProt 263–280 Chain C; UniProt 263–280 Chain D; UniProt 263–280 Chain E; UniProt 263–280 Chain F; UniProt 263–280 Chain G; UniProt 263–280 Chain H; UniProt 263–280 Chain I; UniProt 263–280 Chain J; UniProt 263–280 Chain K; UniProt 263–280 Chain L; UniProt 263–280 Chain M; UniProt 263–280 Chain N; UniProt 263–280 Chain O; UniProt 263–280 Chain P; UniProt 263–280 Chain Q; UniProt 263–280 Chain R; UniProt 263–280 Chain S; UniProt 263–280 Chain T; UniProt 263–280 Chain U; UniProt 263–280 Chain V; UniProt 263–280 Chain W; UniProt 263–280 Chain X; UniProt 263–280 Chain a; UniProt 263–280 Chain b; UniProt 263–280 Chain c; UniProt 263–280 Chain d; UniProt 263–280 Chain e; UniProt 263–280 Chain f; UniProt 263–280 Chain g; UniProt 263–280 Chain h; UniProt 263–280 Chain i; UniProt 263–280 Chain j; UniProt 263–280 Chain k; UniProt 263–280 Chain l; UniProt 263–280 Chain m; UniProt 263–280 Chain n; UniProt 263–280 Chain o; UniProt 263–280 Chain p; UniProt 263–280 Chain q; UniProt 263–280 Chain r; UniProt 263–280 Chain s; UniProt 263–280 Chain t; UniProt 263–280 Chain u; UniProt 263–280 Chain v; UniProt 263–280 Chain w; UniProt 263–280 Chain x; UniProt 263–280 Fragment:acetylated repeat 1 and 2 fragment (AcR1R2) Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4;This is PBS (1x) cryo-EM vitrification conditions:Cryogen ETHANE;We used blot-force of -5, and blot-time of 4 seconds. Resolution 3.88 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 1
Chains and sequence ranges Author chain A; PDBConstruct 2–19; UniProt 263–280 Author chain B; PDBConstruct 2–19; UniProt 263–280 Author chain C; PDBConstruct 2–19; UniProt 263–280 Author chain D; PDBConstruct 2–19; UniProt 263–280 Author chain E; PDBConstruct 2–19; UniProt 263–280 Author chain F; PDBConstruct 2–19; UniProt 263–280 Author chain G; PDBConstruct 2–19; UniProt 263–280 Author chain H; PDBConstruct 2–19; UniProt 263–280 Author chain I; PDBConstruct 2–19; UniProt 263–280 Author chain J; PDBConstruct 2–19; UniProt 263–280 Author chain K; PDBConstruct 2–19; UniProt 263–280 Author chain L; PDBConstruct 2–19; UniProt 263–280 Author chain M; PDBConstruct 2–19; UniProt 263–280 Author chain N; PDBConstruct 2–19; UniProt 263–280 Author chain O; PDBConstruct 2–19; UniProt 263–280 Author chain P; PDBConstruct 2–19; UniProt 263–280 Author chain Q; PDBConstruct 2–19; UniProt 263–280 Author chain R; PDBConstruct 2–19; UniProt 263–280 Author chain S; PDBConstruct 2–19; UniProt 263–280 Author chain T; PDBConstruct 2–19; UniProt 263–280 Author chain U; PDBConstruct 2–19; UniProt 263–280 Author chain V; PDBConstruct 2–19; UniProt 263–280 Author chain W; PDBConstruct 2–19; UniProt 263–280 Author chain X; PDBConstruct 2–19; UniProt 263–280 Author chain a; PDBConstruct 2–19; UniProt 263–280 Author chain b; PDBConstruct 2–19; UniProt 263–280 Author chain c; PDBConstruct 2–19; UniProt 263–280 Author chain d; PDBConstruct 2–19; UniProt 263–280 Author chain e; PDBConstruct 2–19; UniProt 263–280 Author chain f; PDBConstruct 2–19; UniProt 263–280 Author chain g; PDBConstruct 2–19; UniProt 263–280 Author chain h; PDBConstruct 2–19; UniProt 263–280 Author chain i; PDBConstruct 2–19; UniProt 263–280 Author chain j; PDBConstruct 2–19; UniProt 263–280 Author chain k; PDBConstruct 2–19; UniProt 263–280 Author chain l; PDBConstruct 2–19; UniProt 263–280 Author chain m; PDBConstruct 2–19; UniProt 263–280 Author chain n; PDBConstruct 2–19; UniProt 263–280 Author chain o; PDBConstruct 2–19; UniProt 263–280 Author chain p; PDBConstruct 2–19; UniProt 263–280 Author chain q; PDBConstruct 2–19; UniProt 263–280 Author chain r; PDBConstruct 2–19; UniProt 263–280 Author chain s; PDBConstruct 2–19; UniProt 263–280 Author chain t; PDBConstruct 2–19; UniProt 263–280 Author chain u; PDBConstruct 2–19; UniProt 263–280 Author chain v; PDBConstruct 2–19; UniProt 263–280 Author chain w; PDBConstruct 2–19; UniProt 263–280 Author chain x; PDBConstruct 2–19; UniProt 263–280

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 8fnz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8fnz
Deposition date deposition_date2022-12-29
Structure title titleAcetylated tau repeat 1 and 2 fragment (AcR1R2)
Keywords keywordsAmyloid motif acetylation tau repeat domain post-translational modification, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.47
Radius of gyration Rg (electron density) rg_electron35.23
Forward intensity I(0) i049640600.00
Molecular weight molecular_weight58413.0 kDa
Excluded volume excluded_volume74738 ų
Envelope volume envelope_volume91870 ų
Hydration-shell volume shell_volume24826 ų
Envelope diameter envelope_diameter130.3
Shell Rg shell_rg36.21
Envelope Rg envelope_rg35.57
Shape Rg shape_rg35.18
Total Rg total_rg35.49
Total atoms total_atoms4096
Residues n_residues408
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 dmax124.1
Rg (real space) rg_real35.02
Rg uncertainty (real space) rg_real_error1.27
I(0) (real space) i0_real4.9640e+07
I(0) uncertainty (real space) i0_real_error8.7040e+05
Rg (reciprocal space) rg_reciprocal34.68
I(0) (reciprocal space) i0_reciprocal49630000.0000
Solution quality estimate total_estimate0.7449
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.614
Kurtosis Kurtosis kurtosis-0.349
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3265000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.508; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.332; Smooth: 0.824

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)