7nxx

Structure of Superoxide Dismutase 1 (SOD1) in complex with nanobody 2 (Nb2).

Method: X-RAY DIFFRACTION Dmax: 87.2 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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 2–154 Not recorded nanobody 2 × 2 CU COPPER (II) ION × 2 ZN ZINC ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;273 K;0.1 M Hepes,1.5 M Lithium sulphate, pH 7.5 Resolution 2.19 Å R-free 0.245

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 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 7nxx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7nxx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7nxx
Deposition date deposition_date2021-03-19
Structure title titleStructure of Superoxide Dismutase 1 (SOD1) in complex with nanobody 2 (Nb2).
Keywords keywords;Cu/Zn superoxide dismutase metalloenzyme binding catalysing the dismutation of superoxides into hydrogen peroxide, METAL BINDING PROTEIN ;; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.96
Radius of gyration Rg (electron density) rg_electron23.48
Forward intensity I(0) i018647800.00
Molecular weight molecular_weight30631.0 kDa
Excluded volume excluded_volume37378 ų
Envelope volume envelope_volume45687 ų
Hydration-shell volume shell_volume17781 ų
Envelope diameter envelope_diameter90.3
Shell Rg shell_rg28.27
Envelope Rg envelope_rg23.94
Shape Rg shape_rg23.50
Total Rg total_rg24.00
Total atoms total_atoms2145
Residues n_residues289
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 dmax87.2
Rg (real space) rg_real24.28
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.8650e+07
I(0) uncertainty (real space) i0_real_error3.0090e+05
Rg (reciprocal space) rg_reciprocal24.20
I(0) (reciprocal space) i0_reciprocal18650000.0000
Solution quality estimate total_estimate0.7644
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.586
Kurtosis Kurtosis kurtosis-0.272
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2992000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.533; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.391; Smooth: 0.943

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7nxxA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily200 — Superoxide dismutase, copper/zinc binding domain
Domain ID domain_id7nxxB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)