9mil

Superoxide dismutase residues 28-39 with G37R mutation

Method: X-RAY DIFFRACTION Dmax: 63.0 Å Quality: GOOD

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

Superoxide dismutase [Cu-Zn]

OrganismNot specified

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 29–40 Chain B; UniProt 29–40 Chain C; UniProt 29–40 Chain D; UniProt 29–40 Chain E; UniProt 29–40 Chain F; UniProt 29–40 Chain G; UniProt 29–40 Chain H; UniProt 29–40 Chain I; UniProt 29–40 Chain J; UniProt 29–40 Not recorded SO4 SULFATE ION × 5 PG4 TETRAETHYLENE GLYCOL × 2 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;298 K;1.0 M Ammonium sulfate, 0.1 M BIS-TRIS pH 5.5, 1% w/v Polyethylene glycol 3,350 Resolution 2.50 Å R-free 0.263

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 1–12; UniProt 29–40 Author chain B; PDBConstruct 1–12; UniProt 29–40 Author chain C; PDBConstruct 1–12; UniProt 29–40 Author chain D; PDBConstruct 1–12; UniProt 29–40 Author chain E; PDBConstruct 1–12; UniProt 29–40 Author chain F; PDBConstruct 1–12; UniProt 29–40 Author chain G; PDBConstruct 1–12; UniProt 29–40 Author chain H; PDBConstruct 1–12; UniProt 29–40 Author chain I; PDBConstruct 1–12; UniProt 29–40 Author chain J; PDBConstruct 1–12; UniProt 29–40

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 9mil

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9mil
Deposition date deposition_date2024-12-13
Structure title titleSuperoxide dismutase residues 28-39 with G37R mutation
Keywords keywordsCorkescrew, amyloid oligomer, PROTEIN FIBRIL; PROTEIN FIBRIL
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.05
Radius of gyration Rg (electron density) rg_electron16.36
Forward intensity I(0) i03700680.00
Molecular weight molecular_weight14842.0 kDa
Excluded volume excluded_volume19287 ų
Envelope volume envelope_volume22983 ų
Hydration-shell volume shell_volume12653 ų
Envelope diameter envelope_diameter61.3
Shell Rg shell_rg21.38
Envelope Rg envelope_rg16.86
Shape Rg shape_rg16.33
Total Rg total_rg17.51
Total atoms total_atoms1038
Residues n_residues120
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 dmax63.0
Rg (real space) rg_real17.12
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real3.7010e+06
I(0) uncertainty (real space) i0_real_error4.9570e+04
Rg (reciprocal space) rg_reciprocal17.11
I(0) (reciprocal space) i0_reciprocal3701000.0000
Solution quality estimate total_estimate0.8095
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.1
Skewness Skewness skewness0.538
Kurtosis Kurtosis kurtosis0.173
Angular range angular_range— – 0.4650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha773200.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.552; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.866; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)