2wko

Structure of metal loaded Pathogenic SOD1 Mutant G93A.

Method: X-RAY DIFFRACTION Dmax: 70.3 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2–154 Chain F; UniProt 2–154 Fragment:RESIDUES 2-154 Mutation:YES Non-standard monomer:Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 2 ZN ZINC ION × 2 IOD IODIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.5;20% P3350, 0.2 M AMMONIUM IODIDE, pH 6.5 Resolution 1.97 Å R-free 0.231

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 2–154; UniProt 2–154 Author chain F; PDBConstruct 2–154; UniProt 2–154

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 2wko

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2wko
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2wko
Deposition date deposition_date2009-06-16
Structure title titleStructure of metal loaded Pathogenic SOD1 Mutant G93A.
Keywords keywords;AMYOTROPHIC LATERAL SCLEROSIS, PHOSPHOPROTEIN, OXIDOREDUCTASE, DISEASE MUTATION, NEURODEGENERATION, ACETYLATION, ANTIOXIDANT, METAL-BINDING ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.11
Radius of gyration Rg (electron density) rg_electron20.06
Forward intensity I(0) i021671400.00
Molecular weight molecular_weight32341.0 kDa
Excluded volume excluded_volume39093 ų
Envelope volume envelope_volume46744 ų
Hydration-shell volume shell_volume19847 ų
Envelope diameter envelope_diameter72.5
Shell Rg shell_rg26.24
Envelope Rg envelope_rg20.33
Shape Rg shape_rg20.03
Total Rg total_rg20.91
Total atoms total_atoms2234
Residues n_residues305
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 dmax70.3
Rg (real space) rg_real21.11
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real2.1670e+07
I(0) uncertainty (real space) i0_real_error2.9300e+05
Rg (reciprocal space) rg_reciprocal21.11
I(0) (reciprocal space) i0_reciprocal21670000.0000
Solution quality estimate total_estimate0.8882
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.8
Skewness Skewness skewness0.341
Kurtosis Kurtosis kurtosis-0.396
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2553000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2wkoa_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.8 — Cu,Zn superoxide dismutase-like
Family Family familyb.1.8.1 — Cu,Zn superoxide dismutase-like
Domain ID domain_idd2wkof_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.8 — Cu,Zn superoxide dismutase-like
Family Family familyb.1.8.1 — Cu,Zn superoxide dismutase-like

CATH v4.4 (2 domains)

Domain ID domain_id2wkoA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id2wkoF00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain

8. Citations (1)

9. Files and Curves (10)