7s21

M. xanthus encapsulin shell protein EncA with T=1 symmetry

Method: ELECTRON MICROSCOPY Dmax: 79.8 Å Quality: REASONABLE

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

EncA

Myxococcus xanthus

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 homooligomer Homooligomer Protein × 60 PDB declaration: 60-meric(60) Consistent with protein copy count Chain A; UniProt 1–294 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3;20 mM HEPES, pH 7.3, 150 mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–294 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3;20 mM HEPES, pH 7.3, 150 mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å
3 Protein homooligomer Homooligomer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–294 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3;20 mM HEPES, pH 7.3, 150 mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å
4 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–294 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3;20 mM HEPES, pH 7.3, 150 mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 Å
5 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–294 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3;20 mM HEPES, pH 7.3, 150 mM NaCl cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 Q1D6H4_MYXXD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–301; UniProt 1–294

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 7s21

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7s21
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7s21
Deposition date deposition_date2021-09-02
Structure title titleM. xanthus encapsulin shell protein EncA with T=1 symmetry
Keywords keywordsencapsulin, nanocage, iron storage, bacterial nano-compartment, CYTOSOLIC PROTEIN, 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_guinier23.64
Radius of gyration Rg (electron density) rg_electron22.98
Forward intensity I(0) i015011300.00
Molecular weight molecular_weight28962.0 kDa
Excluded volume excluded_volume36243 ų
Envelope volume envelope_volume46505 ų
Hydration-shell volume shell_volume18459 ų
Envelope diameter envelope_diameter83.7
Shell Rg shell_rg27.89
Envelope Rg envelope_rg23.72
Shape Rg shape_rg23.00
Total Rg total_rg23.63
Total atoms total_atoms2041
Residues n_residues265
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 dmax79.8
Rg (real space) rg_real23.80
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real1.5010e+07
I(0) uncertainty (real space) i0_real_error2.1680e+05
Rg (reciprocal space) rg_reciprocal23.76
I(0) (reciprocal space) i0_reciprocal15010000.0000
Solution quality estimate total_estimate0.6165
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.462
Kurtosis Kurtosis kurtosis-0.444
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3110000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.788; Stabil: 0.999; Sysdev: 0.286; Positv: 1.000; Valcen: 0.793; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7s21A01
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)