1ts5

I140T MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS

Method: X-RAY DIFFRACTION Dmax: 86.3 Å Quality: GOOD

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

TOXIC SHOCK SYNDROME TOXIN-1

Staphylococcus aureus

UniProt P06886

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 41–234 Mutation:I140T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 4;pH 4 Resolution 3.10 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 41–234 Mutation:I140T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 4;pH 4 Resolution 3.10 Å

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.

11 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TSST_STAAU
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–194; UniProt 41–234 Author chain B; PDBConstruct 1–194; UniProt 41–234

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 1ts5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ts5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ts5
Deposition date deposition_date1997-10-10
Structure title titleI140T MUTANT OF TOXIC SHOCK SYNDROME TOXIN-1 FROM S. AUREUS
Keywords keywordsTOXIN, SUPERANTIGEN; TOXIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.32
Radius of gyration Rg (electron density) rg_electron25.46
Forward intensity I(0) i032172100.00
Molecular weight molecular_weight44124.0 kDa
Excluded volume excluded_volume55382 ų
Envelope volume envelope_volume69006 ų
Hydration-shell volume shell_volume23378 ų
Envelope diameter envelope_diameter93.4
Shell Rg shell_rg31.74
Envelope Rg envelope_rg25.45
Shape Rg shape_rg25.44
Total Rg total_rg26.27
Total atoms total_atoms3116
Residues n_residues388
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 dmax86.3
Rg (real space) rg_real26.37
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real3.2170e+07
I(0) uncertainty (real space) i0_real_error4.4240e+05
Rg (reciprocal space) rg_reciprocal26.36
I(0) (reciprocal space) i0_reciprocal32170000.0000
Solution quality estimate total_estimate0.8942
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.3
Skewness Skewness skewness0.354
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.3000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4014000.0000
Real-space data points n_real_points61
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.919; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1ts5a1
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_idd1ts5a2
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
Domain ID domain_idd1ts5b1
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_idd1ts5b2
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 (4 domains)

Domain ID domain_id1ts5A01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily120
Domain ID domain_id1ts5A02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110
Domain ID domain_id1ts5B01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily120
Domain ID domain_id1ts5B02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology50 — OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Homologous superfamily homologous superfamily110

8. Citations (3)

9. Files and Curves (10)