1kmg

The Solution Structure Of Monomeric Copper-free Superoxide Dismutase

Method: SOLUTION NMR Dmax: 46.7 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Superoxide Dismutase

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 1–153 Mutation:C6A, F50E, G51E, C111S, E133Q ZN ZINC ION × 1 SOLUTION NMR NMR measurement conditions:pH 5;298 K;Ionic strength (raw mmCIF value) 20 mM phosphate;Pressure 1 NMR sample composition:2mM of 15N and 13C enriched superoxide dismutase | 20mM phosphate buffer, 10% D20 NMR sample composition:2mM of 15N and 13C enriched superoxide dismutase | 20mM phosphate buffer, 10% D20 NMR sample composition:2mM unlabelled superoxide dismutase | 20mM phosphate buffer, 10% D20 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

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 1kmg

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1kmg
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1kmg
Deposition date deposition_date2001-12-15
Structure title titleThe Solution Structure Of Monomeric Copper-free Superoxide Dismutase
Keywords keywordsoxidoreductase, superoxide dismutase, copper-free protein, beta-barrel; OXIDOREDUCTASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.37
Radius of gyration Rg (electron density) rg_electron14.32
Forward intensity I(0) i04886380000.00
Molecular weight molecular_weight555370.0 kDa
Excluded volume excluded_volume678610 ų
Envelope volume envelope_volume32958 ų
Hydration-shell volume shell_volume16791 ų
Envelope diameter envelope_diameter51.4
Shell Rg shell_rg22.56
Envelope Rg envelope_rg16.46
Shape Rg shape_rg14.29
Total Rg total_rg14.48
Total atoms total_atoms76755
Residues n_residues5355
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 dmax46.7
Rg (real space) rg_real14.26
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real4.8860e+09
I(0) uncertainty (real space) i0_real_error5.5850e+07
Rg (reciprocal space) rg_reciprocal14.27
I(0) (reciprocal space) i0_reciprocal4886000000.0000
Solution quality estimate total_estimate0.7433
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.016
Kurtosis Kurtosis kurtosis-0.512
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha338400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 0.368; Positv: 1.000; Valcen: 1.000; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1kmga_
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 (1 domains)

Domain ID domain_id1kmgA00
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)