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1ste

STAPHYLOCOCCAL ENTEROTOXIN C2 FROM STAPHYLOCOCCUS AUREUS

Method: X-RAY DIFFRACTION Dmax: 62.1 Å Quality: GOOD
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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 ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 6.5；pH 6.5 Resolution 2.00 Å R-free 0.255

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.

Other PDB Difference from Current Entry 1STE Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1CQV CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN C2 AT 100K CRYSTALLIZED AT PH 5.0 Deposited 1999-08-11 Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–266（239 aa）
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
1I4P CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN C2 AT 100K CRYSTALLIZED AT PH 5.5 Deposited 2001-02-22 Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–266（239 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298 K；PEG 8000, magnesium Acetate, cacodylate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.00 Å R-free 0.263
1I4Q CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN C2 AT 100K CRYSTALLIZED AT PH 6.0 Deposited 2001-02-22 Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–266（239 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6；PEG 8000, magnesium acetate, cacodylate, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 100K
Resolution 2.20 Å R-free 0.254
1I4R CRYSTAL STRUCTURE OF STAPHYLOCOCCAL ENTEROTOXIN C2 AT 100K CRYSTALLIZED AT PH 6.5 Deposited 2001-02-22 Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–266（239 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；PEG 8000, magnesium acetate, cacodylate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 100K
Resolution 2.10 Å R-free 0.243
1I4X STAPHYLOCOCCAL ENTEROTOXIN C2, MONOCLINIC FORM CRYSTALLIZED AT PH 8.0 Deposited 2001-02-23 Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–266（239 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；291 K；PEG 6000, Tris, pH 8.00, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.40 Å
1SE2 STAPHYLOCOCCAL ENTEROTOXIN C2, MONOCLINIC FORM Deposited 1995-07-20 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–266（239 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.70 Å R-free 0.320
1UNS IDENTIFICATION OF A SECONDARY ZINC-BINDING SITE IN STAPHYLOCOCCAL ENTEROTOXIN C2: IMPLICATIONS FOR SUPERANTIGEN RECOGNITION Deposited 2003-09-15 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 28–266（239 aa）
Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.50
Resolution 2.00 Å R-free 0.225
9XZX Staphylococcal Enterotoxin C in complex with NB C107 and NB C112 Deposited 2025-08-27 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 31–266（236 aa）
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å

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 1ste

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1ste
Deposition date deposition_date1995-08-21
Structure title titleSTAPHYLOCOCCAL ENTEROTOXIN C2 FROM STAPHYLOCOCCUS AUREUS
Keywords keywordsSUPERANTIGEN, TOXIN, ENTEROTOXIN; ENTEROTOXIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier18.97 Å
Radius of gyration Rg (electron density) rg_electron17.78 Å
Forward intensity I(0) i013299000.00
Molecular weight molecular_weight27065.0 kDa
Excluded volume excluded_volume33669 ų
Envelope volume envelope_volume38921 ų
Hydration-shell volume shell_volume18177 ų
Envelope diameter envelope_diameter64.8 Å
Shell Rg shell_rg24.11 Å
Envelope Rg envelope_rg18.08 Å
Shape Rg shape_rg17.77 Å
Total Rg total_rg18.74 Å
Total atoms total_atoms1903
Residues n_residues238
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax62.1 Å
Rg (real space) rg_real18.87 Å
Rg uncertainty (real space) rg_real_error0.28 Å
I(0) (real space) i0_real1.3300e+07
I(0) uncertainty (real space) i0_real_error1.7260e+05
Rg (reciprocal space) rg_reciprocal18.88 Å
I(0) (reciprocal space) i0_reciprocal13300000.0000
Solution quality estimate total_estimate0.8131
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3 Å
Skewness Skewness skewness0.180
Kurtosis Kurtosis kurtosis-0.417
Angular range angular_range— – 0.4200 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha2795000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1stea1
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_idd1stea2
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_id1steA01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110 —
Domain ID domain_id1steA02
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily120 —
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8. Citations (4)

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9. Files and Curves (10)