2af2

Solution structure of disulfide reduced and copper depleted Human Superoxide Dismutase

Method: SOLUTION NMR Dmax: 63.9 Å Quality: REASONABLE

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 1–153 Chain B; UniProt 1–153 Mutation:C6A, C111S ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 5;298 K;Ionic strength (raw mmCIF value) 20mM sodium phosphate;Pressure 1 NMR sample composition:1.5mM 15N protein sample | 20mM sodium phosphate, 20mM DTT buffer, pH 5, 90% H2O, 10% D2O NMR sample composition:1mM 15N;13C protein sample | 20mM sodium phosphate, 20mM DTT buffer, pH 5, 90% H2O, 10% D2O NMR sample composition:1mM 15N;13C;2H protein sample. The triple labeled dimeric SOD contained about 70% 2H | 20mM sodium phosphate, 20mM DTT, buffer, pH 5, 90% H2O, 10% D2O Resolution not provided

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 1–153; UniProt 1–153 Author chain B; PDBConstruct 1–153; UniProt 1–153

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 2af2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2af2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2af2
Deposition date deposition_date2005-07-25
Structure title titleSolution structure of disulfide reduced and copper depleted Human Superoxide Dismutase
Keywords keywords;Human superoxide dismutase, solution structure, homodimeric protein, disulfide bond reduced, copper depleted protein, Structural Genomics, Structural Proteomics in Europe, SPINE, Oxidoreductase ;; OXIDOREDUCTASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier19.99
Radius of gyration Rg (electron density) rg_electron19.73
Forward intensity I(0) i013999500000.00
Molecular weight molecular_weight947930.0 kDa
Excluded volume excluded_volume1161100 ų
Envelope volume envelope_volume67658 ų
Hydration-shell volume shell_volume25834 ų
Envelope diameter envelope_diameter73.9
Shell Rg shell_rg29.03
Envelope Rg envelope_rg21.78
Shape Rg shape_rg19.72
Total Rg total_rg19.83
Total atoms total_atoms131250
Residues n_residues9180
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 dmax63.9
Rg (real space) rg_real19.97
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real1.4000e+10
I(0) uncertainty (real space) i0_real_error1.6150e+08
Rg (reciprocal space) rg_reciprocal19.97
I(0) (reciprocal space) i0_reciprocal14000000000.0000
Solution quality estimate total_estimate0.7031
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.309
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1753000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.900; Stabil: 0.999; Sysdev: 0.210; Positv: 1.000; Valcen: 0.987; Smooth: 0.822

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2af2a_
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_idd2af2b_
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_id2af2A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id2af2B00
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)