5iiw

Corkscrew assembly of SOD1 residues 28-38 without potassium iodide

Method: X-RAY DIFFRACTION Dmax: 70.6 Å Quality: REASONABLE

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 29–39 Chain B; UniProt 29–39 Chain C; UniProt 29–39 Chain D; UniProt 29–39 Chain E; UniProt 29–39 Chain F; UniProt 29–39 Chain G; UniProt 29–39 Chain H; UniProt 29–39 Fragment:UNP Residues 29-39 Mutation:P29K No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;298 K;reservoir contained 13% PEG 6000, 0.2M Sodium Citrate Resolution 2.00 Å R-free 0.252

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 1–11; UniProt 29–39 Author chain B; PDBConstruct 1–11; UniProt 29–39 Author chain C; PDBConstruct 1–11; UniProt 29–39 Author chain D; PDBConstruct 1–11; UniProt 29–39 Author chain E; PDBConstruct 1–11; UniProt 29–39 Author chain F; PDBConstruct 1–11; UniProt 29–39 Author chain G; PDBConstruct 1–11; UniProt 29–39 Author chain H; PDBConstruct 1–11; UniProt 29–39

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 5iiw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5iiw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5iiw
Deposition date deposition_date2016-03-01
Structure title titleCorkscrew assembly of SOD1 residues 28-38 without potassium iodide
Keywords keywordsamyloid-related oligomer, UNKNOWN FUNCTION; UNKNOWN FUNCTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.59
Radius of gyration Rg (electron density) rg_electron16.02
Forward intensity I(0) i01445390.00
Molecular weight molecular_weight9740.0 kDa
Excluded volume excluded_volume13077 ų
Envelope volume envelope_volume15269 ų
Hydration-shell volume shell_volume9366 ų
Envelope diameter envelope_diameter67.7
Shell Rg shell_rg19.60
Envelope Rg envelope_rg16.82
Shape Rg shape_rg15.97
Total Rg total_rg17.13
Total atoms total_atoms688
Residues n_residues88
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 dmax70.6
Rg (real space) rg_real16.93
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.4450e+06
I(0) uncertainty (real space) i0_real_error2.0200e+04
Rg (reciprocal space) rg_reciprocal16.89
I(0) (reciprocal space) i0_reciprocal1445000.0000
Solution quality estimate total_estimate0.6838
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.6
Skewness Skewness skewness0.781
Kurtosis Kurtosis kurtosis0.501
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha246700.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.274; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.119; Smooth: 0.944

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)