9bc8

Cargo-loaded Myxococcus xanthus EncA encapsulin engineered pore mutant with T=4 icosahedral symmetry

Method: ELECTRON MICROSCOPY Dmax: 159.1 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 × 480 PDB declaration: 480-meric(480) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Chain D; UniProt 1–287 Mutation:I203G, Y204G Encapsulin nanocompartment cargo protein EncC × 240 (Q1D3Y8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 Å
2 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Chain D; UniProt 1–287 Mutation:I203G, Y204G Encapsulin nanocompartment cargo protein EncC × 4 (Q1D3Y8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 Å
3 Protein heterocomplex Heteromer Protein × 40 PDB declaration: 40-meric(40) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Chain D; UniProt 1–287 Mutation:I203G, Y204G Encapsulin nanocompartment cargo protein EncC × 20 (Q1D3Y8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 Å
4 Protein heterocomplex Heteromer Protein × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Chain D; UniProt 1–287 Mutation:I203G, Y204G Encapsulin nanocompartment cargo protein EncC × 24 (Q1D3Y8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 Å
5 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–287 Chain B; UniProt 1–287 Chain C; UniProt 1–287 Chain D; UniProt 1–287 Mutation:I203G, Y204G Encapsulin nanocompartment cargo protein EncC × 4 (Q1D3Y8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 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 1–281; UniProt 1–287 Author chain B; PDBConstruct 1–281; UniProt 1–287 Author chain C; PDBConstruct 1–281; UniProt 1–287 Author chain D; PDBConstruct 1–281; UniProt 1–287

Encapsulin nanocompartment cargo protein EncC

Myxococcus xanthus DK 1622

UniProt Q1D3Y8

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 × 480 PDB declaration: 480-meric(480) Consistent with protein copy count Chain E; UniProt 119–130 Chain F; UniProt 119–130 Chain G; UniProt 119–130 Chain H; UniProt 119–130 Fragment:C-terminal targeting peptide (UNP residues 119-130) Type 1 encapsulin shell protein EncA × 240 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 Å
2 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 119–130 Chain F; UniProt 119–130 Chain G; UniProt 119–130 Chain H; UniProt 119–130 Fragment:C-terminal targeting peptide (UNP residues 119-130) Type 1 encapsulin shell protein EncA × 4 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 Å
3 Protein heterocomplex Heteromer Protein × 40 PDB declaration: 40-meric(40) Consistent with protein copy count Chain E; UniProt 119–130 Chain F; UniProt 119–130 Chain G; UniProt 119–130 Chain H; UniProt 119–130 Fragment:C-terminal targeting peptide (UNP residues 119-130) Type 1 encapsulin shell protein EncA × 20 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 Å
4 Protein heterocomplex Heteromer Protein × 48 PDB declaration: 48-meric(48) Consistent with protein copy count Chain E; UniProt 119–130 Chain F; UniProt 119–130 Chain G; UniProt 119–130 Chain H; UniProt 119–130 Fragment:C-terminal targeting peptide (UNP residues 119-130) Type 1 encapsulin shell protein EncA × 24 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 Å
5 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 119–130 Chain F; UniProt 119–130 Chain G; UniProt 119–130 Chain H; UniProt 119–130 Fragment:C-terminal targeting peptide (UNP residues 119-130) Type 1 encapsulin shell protein EncA × 4 (Q1D6H4) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl, 20 mM Tris pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force: 20 Blot time: 4 seconds Wait time: 0 seconds Resolution 3.46 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.

2 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ENCC_MYXXD
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–12; UniProt 119–130 Author chain F; PDBConstruct 1–12; UniProt 119–130 Author chain G; PDBConstruct 1–12; UniProt 119–130 Author chain H; PDBConstruct 1–12; UniProt 119–130

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 9bc8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9bc8
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9bc8
Deposition date deposition_date2024-04-08
最后修订 last_revision2024-10-30
Structure title titleCargo-loaded Myxococcus xanthus EncA encapsulin engineered pore mutant with T=4 icosahedral symmetry
Keywords keywordsencapsulin, nanocompartment, pore mutant, 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_guinier42.85
Radius of gyration Rg (electron density) rg_electron42.95
Forward intensity I(0) i0238702000.00
Molecular weight molecular_weight124090.0 kDa
Excluded volume excluded_volume154880 ų
Envelope volume envelope_volume222810 ų
Hydration-shell volume shell_volume46736 ų
Envelope diameter envelope_diameter166.2
Shell Rg shell_rg43.10
Envelope Rg envelope_rg43.82
Shape Rg shape_rg42.97
Total Rg total_rg42.92
Total atoms total_atoms8740
Residues n_residues1128
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 dmax159.1
Rg (real space) rg_real43.08
Rg uncertainty (real space) rg_real_error1.90
I(0) (real space) i0_real2.3870e+08
I(0) uncertainty (real space) i0_real_error4.6220e+06
Rg (reciprocal space) rg_reciprocal42.86
I(0) (reciprocal space) i0_reciprocal238600000.0000
Solution quality estimate total_estimate0.8307
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.7
Skewness Skewness skewness0.393
Kurtosis Kurtosis kurtosis-0.425
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24680000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.700; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.732; Smooth: 0.962

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)