1se2

STAPHYLOCOCCAL ENTEROTOXIN C2, MONOCLINIC FORM

Method: X-RAY DIFFRACTION Dmax: 62.1 Å Quality: REASONABLE

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

STAPHYLOCOCCAL ENTEROTOXIN C2

OrganismNot specified

UniProt P34071

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 28–266 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.70 Å R-free 0.320

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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENTC2_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–239; UniProt 28–266

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 1se2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1se2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1se2
Deposition date deposition_date1995-07-20
Structure title titleSTAPHYLOCOCCAL ENTEROTOXIN C2, MONOCLINIC FORM
Keywords keywordsENTEROTOXIN, SUPERANTIGEN, TOXIN; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.97
Radius of gyration Rg (electron density) rg_electron17.77
Forward intensity I(0) i013491300.00
Molecular weight molecular_weight27198.0 kDa
Excluded volume excluded_volume33866 ų
Envelope volume envelope_volume38455 ų
Hydration-shell volume shell_volume17986 ų
Envelope diameter envelope_diameter63.8
Shell Rg shell_rg24.19
Envelope Rg envelope_rg18.15
Shape Rg shape_rg17.75
Total Rg total_rg18.79
Total atoms total_atoms1914
Residues n_residues235
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 dmax62.1
Rg (real space) rg_real18.88
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.3490e+07
I(0) uncertainty (real space) i0_real_error1.6470e+05
Rg (reciprocal space) rg_reciprocal18.89
I(0) (reciprocal space) i0_reciprocal13490000.0000
Solution quality estimate total_estimate0.6650
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.1
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.355
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3129000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.840; Stabil: 0.999; Sysdev: 0.374; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1se2a1
Class classb — All beta proteins
Fold Fold foldb.40 — OB-fold
Superfamily Superfamily superfamilyb.40.2 — Bacterial enterotoxins
Family Family familyb.40.2.2 — Superantigen toxins, N-terminal domain
Domain ID domain_idd1se2a2
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.6 — Superantigen toxins, C-terminal domain
Family Family familyd.15.6.1 — Superantigen toxins, C-terminal domain

CATH v4.4 (2 domains)

Domain ID domain_id1se2A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1se2A02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily120

8. Citations (2)

9. Files and Curves (10)