8ihu

Cryo-EM structure of an amyloid fibril formed by ALS-causing SOD1 mutation G85R

Method: ELECTRON MICROSCOPY Dmax: 74.6 Å Quality: GOOD

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

Superoxide dismutase [Cu-Zn]

Homo sapiens

UniProt P00441

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–154 Chain B; UniProt 1–154 Chain C; UniProt 1–154 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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.

153 other PDB entries and 375 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SODC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–154; UniProt 1–154 Author chain B; PDBConstruct 1–154; UniProt 1–154 Author chain C; PDBConstruct 1–154; UniProt 1–154

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 8ihu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8ihu
Deposition date deposition_date2023-02-23
最后修订 last_revision2024-10-30
Structure title titleCryo-EM structure of an amyloid fibril formed by ALS-causing SOD1 mutation G85R
Keywords keywordsAmyloid fibril, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.45
Radius of gyration Rg (electron density) rg_electron22.19
Forward intensity I(0) i010193900.00
Molecular weight molecular_weight21855.0 kDa
Excluded volume excluded_volume26614 ų
Envelope volume envelope_volume35421 ų
Hydration-shell volume shell_volume14703 ų
Envelope diameter envelope_diameter73.8
Shell Rg shell_rg26.59
Envelope Rg envelope_rg22.20
Shape Rg shape_rg22.18
Total Rg total_rg22.86
Total atoms total_atoms1527
Residues n_residues216
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 dmax74.6
Rg (real space) rg_real22.57
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real1.0190e+07
I(0) uncertainty (real space) i0_real_error1.4380e+05
Rg (reciprocal space) rg_reciprocal22.55
I(0) (reciprocal space) i0_reciprocal10190000.0000
Solution quality estimate total_estimate0.8826
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.0
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha698400.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.889; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.822; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)