9y8p

Cryo-EM structure of Thermotoga maritima encapsulin shell

Method: ELECTRON MICROSCOPY Dmax: 249.0 Å Quality: GOOD

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

Type 1 encapsulin shell protein

Thermotoga maritima

UniProt Q9WZP2

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 × 60 PDB declaration: 60-meric(60) Consistent with protein copy count Chain A; UniProt 1–265 Chain AA; UniProt 1–265 Chain AB; UniProt 1–265 Chain B; UniProt 1–265 Chain BA; UniProt 1–265 Chain BB; UniProt 1–265 Chain C; UniProt 1–265 Chain CA; UniProt 1–265 Chain CB; UniProt 1–265 Chain D; UniProt 1–265 Chain DA; UniProt 1–265 Chain DB; UniProt 1–265 Chain E; UniProt 1–265 Chain EA; UniProt 1–265 Chain EB; UniProt 1–265 Chain F; UniProt 1–265 Chain FA; UniProt 1–265 Chain FB; UniProt 1–265 Chain G; UniProt 1–265 Chain GA; UniProt 1–265 Chain GB; UniProt 1–265 Chain H; UniProt 1–265 Chain HA; UniProt 1–265 Chain HB; UniProt 1–265 Chain I; UniProt 1–265 Chain IA; UniProt 1–265 Chain J; UniProt 1–265 Chain JA; UniProt 1–265 Chain K; UniProt 1–265 Chain KA; UniProt 1–265 Chain L; UniProt 1–265 Chain LA; UniProt 1–265 Chain M; UniProt 1–265 Chain MA; UniProt 1–265 Chain N; UniProt 1–265 Chain NA; UniProt 1–265 Chain O; UniProt 1–265 Chain OA; UniProt 1–265 Chain P; UniProt 1–265 Chain PA; UniProt 1–265 Chain Q; UniProt 1–265 Chain QA; UniProt 1–265 Chain R; UniProt 1–265 Chain RA; UniProt 1–265 Chain S; UniProt 1–265 Chain SA; UniProt 1–265 Chain T; UniProt 1–265 Chain TA; UniProt 1–265 Chain U; UniProt 1–265 Chain UA; UniProt 1–265 Chain V; UniProt 1–265 Chain VA; UniProt 1–265 Chain W; UniProt 1–265 Chain WA; UniProt 1–265 Chain X; UniProt 1–265 Chain XA; UniProt 1–265 Chain Y; UniProt 1–265 Chain YA; UniProt 1–265 Chain Z; UniProt 1–265 Chain ZA; UniProt 1–265 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.80 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.

12 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENCAP_THEMA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–265; UniProt 1–265 Author chain AA; PDBConstruct 1–265; UniProt 1–265 Author chain AB; PDBConstruct 1–265; UniProt 1–265 Author chain B; PDBConstruct 1–265; UniProt 1–265 Author chain BA; PDBConstruct 1–265; UniProt 1–265 Author chain BB; PDBConstruct 1–265; UniProt 1–265 Author chain C; PDBConstruct 1–265; UniProt 1–265 Author chain CA; PDBConstruct 1–265; UniProt 1–265 Author chain CB; PDBConstruct 1–265; UniProt 1–265 Author chain D; PDBConstruct 1–265; UniProt 1–265 Author chain DA; PDBConstruct 1–265; UniProt 1–265 Author chain DB; PDBConstruct 1–265; UniProt 1–265 Author chain E; PDBConstruct 1–265; UniProt 1–265 Author chain EA; PDBConstruct 1–265; UniProt 1–265 Author chain EB; PDBConstruct 1–265; UniProt 1–265 Author chain F; PDBConstruct 1–265; UniProt 1–265 Author chain FA; PDBConstruct 1–265; UniProt 1–265 Author chain FB; PDBConstruct 1–265; UniProt 1–265 Author chain G; PDBConstruct 1–265; UniProt 1–265 Author chain GA; PDBConstruct 1–265; UniProt 1–265 Author chain GB; PDBConstruct 1–265; UniProt 1–265 Author chain H; PDBConstruct 1–265; UniProt 1–265 Author chain HA; PDBConstruct 1–265; UniProt 1–265 Author chain HB; PDBConstruct 1–265; UniProt 1–265 Author chain I; PDBConstruct 1–265; UniProt 1–265 Author chain IA; PDBConstruct 1–265; UniProt 1–265 Author chain J; PDBConstruct 1–265; UniProt 1–265 Author chain JA; PDBConstruct 1–265; UniProt 1–265 Author chain K; PDBConstruct 1–265; UniProt 1–265 Author chain KA; PDBConstruct 1–265; UniProt 1–265 Author chain L; PDBConstruct 1–265; UniProt 1–265 Author chain LA; PDBConstruct 1–265; UniProt 1–265 Author chain M; PDBConstruct 1–265; UniProt 1–265 Author chain MA; PDBConstruct 1–265; UniProt 1–265 Author chain N; PDBConstruct 1–265; UniProt 1–265 Author chain NA; PDBConstruct 1–265; UniProt 1–265 Author chain O; PDBConstruct 1–265; UniProt 1–265 Author chain OA; PDBConstruct 1–265; UniProt 1–265 Author chain P; PDBConstruct 1–265; UniProt 1–265 Author chain PA; PDBConstruct 1–265; UniProt 1–265 Author chain Q; PDBConstruct 1–265; UniProt 1–265 Author chain QA; PDBConstruct 1–265; UniProt 1–265 Author chain R; PDBConstruct 1–265; UniProt 1–265 Author chain RA; PDBConstruct 1–265; UniProt 1–265 Author chain S; PDBConstruct 1–265; UniProt 1–265 Author chain SA; PDBConstruct 1–265; UniProt 1–265 Author chain T; PDBConstruct 1–265; UniProt 1–265 Author chain TA; PDBConstruct 1–265; UniProt 1–265 Author chain U; PDBConstruct 1–265; UniProt 1–265 Author chain UA; PDBConstruct 1–265; UniProt 1–265 Author chain V; PDBConstruct 1–265; UniProt 1–265 Author chain VA; PDBConstruct 1–265; UniProt 1–265 Author chain W; PDBConstruct 1–265; UniProt 1–265 Author chain WA; PDBConstruct 1–265; UniProt 1–265 Author chain X; PDBConstruct 1–265; UniProt 1–265 Author chain XA; PDBConstruct 1–265; UniProt 1–265 Author chain Y; PDBConstruct 1–265; UniProt 1–265 Author chain YA; PDBConstruct 1–265; UniProt 1–265 Author chain Z; PDBConstruct 1–265; UniProt 1–265 Author chain ZA; PDBConstruct 1–265; UniProt 1–265

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 9y8p

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9y8p
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9y8p
Deposition date deposition_date2025-09-11
Structure title titleCryo-EM structure of Thermotoga maritima encapsulin shell
Keywords keywordsENCAPSULIN SHELL, VIRUS LIKE PARTICLE; VIRUS LIKE PARTICLE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron105.50
Forward intensity I(0) i042521000000.00
Molecular weight molecular_weight1827900.0 kDa
Excluded volume excluded_volume2313700 ų
Envelope volume envelope_volume6210100 ų
Hydration-shell volume shell_volume501530 ų
Envelope diameter envelope_diameter248.9
Shell Rg shell_rg116.50
Envelope Rg envelope_rg88.89
Shape Rg shape_rg105.50
Total Rg total_rg105.70
Total atoms total_atoms129180
Residues n_residues15900
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 dmax249.0
Rg (real space) rg_real106.00
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real4.2560e+10
I(0) uncertainty (real space) i0_real_error6.3590e+08
Rg (reciprocal space) rg_reciprocal115.80
I(0) (reciprocal space) i0_reciprocal43910000000.0000
Solution quality estimate total_estimate0.8600
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary182.6
Skewness Skewness skewness-0.481
Kurtosis Kurtosis kurtosis-0.608
Angular range angular_range— – 0.0750 −1
Current regularization parameter α current_alpha1.2500
Highest regularization parameter α highest_alpha8184000000000000.0000
Real-space data points n_real_points16
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.788; Stabil: 0.973; Sysdev: 1.000; Positv: 1.000; Valcen: 0.898; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)