1cqv

CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN C2 AT 100K CRYSTALLIZED AT PH 5.0

Method: X-RAY DIFFRACTION Dmax: 59.7 Å Quality: GOOD

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

PROTEIN (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 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;291 K;20% PEG 8000, 0.2M MAGNESIUM ACETATE, 0.1M CACODYLATE AT PH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.06 Å R-free 0.280

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 1cqv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1cqv
Deposition date deposition_date1999-08-11
Structure title titleCRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN C2 AT 100K CRYSTALLIZED AT PH 5.0
Keywords keywordsENTEROTOXIN, SUPERANTIGEN, ZINC BINDING, IMMUNE SYSTEM, TOXIN; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.78
Radius of gyration Rg (electron density) rg_electron17.53
Forward intensity I(0) i012998500.00
Molecular weight molecular_weight26547.0 kDa
Excluded volume excluded_volume32964 ų
Envelope volume envelope_volume38294 ų
Hydration-shell volume shell_volume18040 ų
Envelope diameter envelope_diameter61.6
Shell Rg shell_rg23.95
Envelope Rg envelope_rg17.87
Shape Rg shape_rg17.51
Total Rg total_rg18.55
Total atoms total_atoms1866
Residues n_residues232
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 dmax59.7
Rg (real space) rg_real18.67
Rg uncertainty (real space) rg_real_error0.23
I(0) (real space) i0_real1.3000e+07
I(0) uncertainty (real space) i0_real_error1.3970e+05
Rg (reciprocal space) rg_reciprocal18.68
I(0) (reciprocal space) i0_reciprocal13000000.0000
Solution quality estimate total_estimate0.8961
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.161
Kurtosis Kurtosis kurtosis-0.449
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3013000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.969

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1cqva1
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_idd1cqva2
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_id1cqvA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1cqvA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily120

8. Citations (3)

9. Files and Curves (10)