2lu5

Structure and chemical shifts of Cu(I),Zn(II) superoxide dismutase by solid-state NMR

Method: SOLID-STATE NMR Dmax: 45.1 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–154 Mutation:C6A, C111S CU COPPER (II) ION × 1 SOLID-STATE NMR NMR measurement conditions:pH 5;286 K;Ionic strength (raw mmCIF value) 0.02;Pressure ambient NMR sample composition:3.5 mg [U-13C; U-15N; U-2H] Superoxide dismutase C6A/C111S thermostable mutant, 20 mM Sodium Citrate, 20% w/v Polyethylene Glycol 6000, 100% H2O | 100% H2O 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 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 2lu5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2lu5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2lu5
Deposition date deposition_date2012-06-08
Structure title titleStructure and chemical shifts of Cu(I),Zn(II) superoxide dismutase by solid-state NMR
Keywords keywordsMetalloprotein, Microcrystalline, Paramagnetic, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodSOLID-STATE NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.89
Radius of gyration Rg (electron density) rg_electron13.93
Forward intensity I(0) i01426620000.00
Molecular weight molecular_weight300470.0 kDa
Excluded volume excluded_volume367900 ų
Envelope volume envelope_volume34756 ų
Hydration-shell volume shell_volume17551 ų
Envelope diameter envelope_diameter50.7
Shell Rg shell_rg22.86
Envelope Rg envelope_rg16.38
Shape Rg shape_rg13.91
Total Rg total_rg14.15
Total atoms total_atoms41705
Residues n_residues2907
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 dmax45.1
Rg (real space) rg_real13.78
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real1.4270e+09
I(0) uncertainty (real space) i0_real_error1.5630e+07
Rg (reciprocal space) rg_reciprocal13.79
I(0) (reciprocal space) i0_reciprocal1427000000.0000
Solution quality estimate total_estimate0.8828
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.3
Skewness Skewness skewness0.084
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha616500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2lu5A00
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)