8tk7

Myxococcus xanthus EncA protein shell with compartmentalized SNAP-tag cargo protein

Method: ELECTRON MICROSCOPY Dmax: 130.3 Å Quality: GOOD

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

Type 1 encapsulin shell protein EncA

Myxococcus xanthus DK 1622

UniProt Q1D6H4

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 heterocomplex Heteromer Protein × 360 PDB declaration: 360-meric(360) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Not recorded Methylated-DNA--protein-cysteine methyltransferase × 180 (E5BBQ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 Å
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Not recorded Methylated-DNA--protein-cysteine methyltransferase × 3 (E5BBQ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 Å
3 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Not recorded Methylated-DNA--protein-cysteine methyltransferase × 15 (E5BBQ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 Å
4 Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Not recorded Methylated-DNA--protein-cysteine methyltransferase × 18 (E5BBQ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Not recorded Methylated-DNA--protein-cysteine methyltransferase × 3 (E5BBQ0) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 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 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENCAP_MYXXD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–287; UniProt 1–287 Author chain B; PDBConstruct 1–287; UniProt 1–287 Author chain C; PDBConstruct 1–287; UniProt 1–287

Methylated-DNA--protein-cysteine methyltransferase

Homo sapiens

UniProt E5BBQ0

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 heterocomplex Heteromer Protein × 360 PDB declaration: 360-meric(360) Consistent with protein copy count Chain D; UniProt 1–182 Chain E; UniProt 1–182 Chain F; UniProt 1–182 Not recorded Type 1 encapsulin shell protein EncA × 180 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 Å
2 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–182 Chain E; UniProt 1–182 Chain F; UniProt 1–182 Not recorded Type 1 encapsulin shell protein EncA × 3 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 Å
3 Protein heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain D; UniProt 1–182 Chain E; UniProt 1–182 Chain F; UniProt 1–182 Not recorded Type 1 encapsulin shell protein EncA × 15 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 Å
4 Protein heterocomplex Heteromer Protein × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain D; UniProt 1–182 Chain E; UniProt 1–182 Chain F; UniProt 1–182 Not recorded Type 1 encapsulin shell protein EncA × 18 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 Å
5 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–182 Chain E; UniProt 1–182 Chain F; UniProt 1–182 Not recorded Type 1 encapsulin shell protein EncA × 3 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.53 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.

7 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E5BBQ0_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 2–183; UniProt 1–182 Author chain E; PDBConstruct 2–183; UniProt 1–182 Author chain F; PDBConstruct 2–183; UniProt 1–182

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 8tk7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tk7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tk7
Deposition date deposition_date2023-07-25
Structure title titleMyxococcus xanthus EncA protein shell with compartmentalized SNAP-tag cargo protein
Keywords keywordsEncapsulin, nanocompartment, 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_guinier36.49
Radius of gyration Rg (electron density) rg_electron36.15
Forward intensity I(0) i0142716000.00
Molecular weight molecular_weight95146.0 kDa
Excluded volume excluded_volume119000 ų
Envelope volume envelope_volume167820 ų
Hydration-shell volume shell_volume40398 ų
Envelope diameter envelope_diameter142.6
Shell Rg shell_rg40.22
Envelope Rg envelope_rg36.49
Shape Rg shape_rg36.16
Total Rg total_rg36.40
Total atoms total_atoms6702
Residues n_residues861
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 dmax130.3
Rg (real space) rg_real36.56
Rg uncertainty (real space) rg_real_error1.03
I(0) (real space) i0_real1.4270e+08
I(0) uncertainty (real space) i0_real_error2.2690e+06
Rg (reciprocal space) rg_reciprocal36.52
I(0) (reciprocal space) i0_reciprocal142700000.0000
Solution quality estimate total_estimate0.8655
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary42.4
Skewness Skewness skewness0.339
Kurtosis Kurtosis kurtosis-0.376
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha24950000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.842; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id8tk7A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily10 — hypothetical protein PF0899 domain
Domain ID domain_id8tk7B01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily10 — hypothetical protein PF0899 domain
Domain ID domain_id8tk7C01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology2320 — hypothetical protein PF0899 fold
Homologous superfamily homologous superfamily10 — hypothetical protein PF0899 domain

8. Citations (1)

9. Files and Curves (10)