9wz3

Cryo-EM structure of the PT domain of EvSS

Method: ELECTRON MICROSCOPY Dmax: 210.4 Å Quality: GOOD

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

Stellatatriene synthase

Aspergillus stellatus

UniProt A0A0P0ZEM1

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 homooligomer Homooligomer Protein × 18 PDB declaration: octadecameric(18) Consistent with protein copy count Chain A; UniProt 1–714 Chain B; UniProt 1–714 Chain C; UniProt 1–714 Chain D; UniProt 1–714 Chain E; UniProt 1–714 Chain F; UniProt 1–714 Chain G; UniProt 1–714 Chain H; UniProt 1–714 Chain I; UniProt 1–714 Chain J; UniProt 1–714 Chain K; UniProt 1–714 Chain L; UniProt 1–714 Chain M; UniProt 1–714 Chain N; UniProt 1–714 Chain O; UniProt 1–714 Chain P; UniProt 1–714 Chain Q; UniProt 1–714 Chain R; UniProt 1–714 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.19 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name STLSS_EMEVA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–714; UniProt 1–714 Author chain B; PDBConstruct 1–714; UniProt 1–714 Author chain C; PDBConstruct 1–714; UniProt 1–714 Author chain D; PDBConstruct 1–714; UniProt 1–714 Author chain E; PDBConstruct 1–714; UniProt 1–714 Author chain F; PDBConstruct 1–714; UniProt 1–714 Author chain G; PDBConstruct 1–714; UniProt 1–714 Author chain H; PDBConstruct 1–714; UniProt 1–714 Author chain I; PDBConstruct 1–714; UniProt 1–714 Author chain J; PDBConstruct 1–714; UniProt 1–714 Author chain K; PDBConstruct 1–714; UniProt 1–714 Author chain L; PDBConstruct 1–714; UniProt 1–714 Author chain M; PDBConstruct 1–714; UniProt 1–714 Author chain N; PDBConstruct 1–714; UniProt 1–714 Author chain O; PDBConstruct 1–714; UniProt 1–714 Author chain P; PDBConstruct 1–714; UniProt 1–714 Author chain Q; PDBConstruct 1–714; UniProt 1–714 Author chain R; PDBConstruct 1–714; UniProt 1–714

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 9wz3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9wz3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9wz3
Deposition date deposition_date2025-09-29
Structure title titleCryo-EM structure of the PT domain of EvSS
Keywords keywordsEvSS, Stellatatriene synthase, BIOSYNTHETIC PROTEIN; BIOSYNTHETIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier71.42
Radius of gyration Rg (electron density) rg_electron72.08
Forward intensity I(0) i05149450000.00
Molecular weight molecular_weight612760.0 kDa
Excluded volume excluded_volume770000 ų
Envelope volume envelope_volume1193300 ų
Hydration-shell volume shell_volume146050 ų
Envelope diameter envelope_diameter242.0
Shell Rg shell_rg64.06
Envelope Rg envelope_rg69.56
Shape Rg shape_rg72.09
Total Rg total_rg71.92
Total atoms total_atoms43146
Residues n_residues5364
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 dmax210.4
Rg (real space) rg_real71.43
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real5.1390e+09
I(0) uncertainty (real space) i0_real_error9.7680e+07
Rg (reciprocal space) rg_reciprocal70.31
I(0) (reciprocal space) i0_reciprocal5135000000.0000
Solution quality estimate total_estimate0.8269
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary76.5
Skewness Skewness skewness0.485
Kurtosis Kurtosis kurtosis-0.434
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0192
Highest regularization parameter α highest_alpha246700000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.011

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)