6mb2

Cryo-EM structure of the PYD filament of AIM2

Method: ELECTRON MICROSCOPY Dmax: 193.9 Å Quality: GOOD

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

Interferon-inducible protein AIM2

Homo sapiens

UniProt O14862

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain A; UniProt 1–93 Chain B; UniProt 1–93 Chain C; UniProt 1–93 Chain D; UniProt 1–93 Chain E; UniProt 1–93 Chain F; UniProt 1–93 Chain G; UniProt 1–93 Chain H; UniProt 1–93 Chain I; UniProt 1–93 Chain J; UniProt 1–93 Chain K; UniProt 1–93 Chain L; UniProt 1–93 Chain M; UniProt 1–93 Chain N; UniProt 1–93 Chain O; UniProt 1–93 Fragment:PYD (UNP residues 1-93) Green fluorescent protein × 15 (P42212) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.00 Å R-free 0.423

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AIM2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–94; UniProt 1–93 Author chain B; PDBConstruct 2–94; UniProt 1–93 Author chain C; PDBConstruct 2–94; UniProt 1–93 Author chain D; PDBConstruct 2–94; UniProt 1–93 Author chain E; PDBConstruct 2–94; UniProt 1–93 Author chain F; PDBConstruct 2–94; UniProt 1–93 Author chain G; PDBConstruct 2–94; UniProt 1–93 Author chain H; PDBConstruct 2–94; UniProt 1–93 Author chain I; PDBConstruct 2–94; UniProt 1–93 Author chain J; PDBConstruct 2–94; UniProt 1–93 Author chain K; PDBConstruct 2–94; UniProt 1–93 Author chain L; PDBConstruct 2–94; UniProt 1–93 Author chain M; PDBConstruct 2–94; UniProt 1–93 Author chain N; PDBConstruct 2–94; UniProt 1–93 Author chain O; PDBConstruct 2–94; UniProt 1–93

Green fluorescent protein

Aequorea victoria

UniProt P42212

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain a; UniProt 2–229 Chain b; UniProt 2–229 Chain c; UniProt 2–229 Chain d; UniProt 2–229 Chain e; UniProt 2–229 Chain f; UniProt 2–229 Chain g; UniProt 2–229 Chain h; UniProt 2–229 Chain i; UniProt 2–229 Chain j; UniProt 2–229 Chain k; UniProt 2–229 Chain l; UniProt 2–229 Chain m; UniProt 2–229 Chain n; UniProt 2–229 Chain o; UniProt 2–229 Fragment:UNP residues 2-229 Non-standard monomer:Yes (specific site not provided by mmCIF) Interferon-inducible protein AIM2 × 15 (O14862) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.00 Å R-free 0.423

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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 2
Chains and sequence ranges Author chain a; PDBConstruct 1–226; UniProt 2–229 Author chain b; PDBConstruct 1–226; UniProt 2–229 Author chain c; PDBConstruct 1–226; UniProt 2–229 Author chain d; PDBConstruct 1–226; UniProt 2–229 Author chain e; PDBConstruct 1–226; UniProt 2–229 Author chain f; PDBConstruct 1–226; UniProt 2–229 Author chain g; PDBConstruct 1–226; UniProt 2–229 Author chain h; PDBConstruct 1–226; UniProt 2–229 Author chain i; PDBConstruct 1–226; UniProt 2–229 Author chain j; PDBConstruct 1–226; UniProt 2–229 Author chain k; PDBConstruct 1–226; UniProt 2–229 Author chain l; PDBConstruct 1–226; UniProt 2–229 Author chain m; PDBConstruct 1–226; UniProt 2–229 Author chain n; PDBConstruct 1–226; UniProt 2–229 Author chain o; PDBConstruct 1–226; UniProt 2–229

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 6mb2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6mb2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6mb2
Deposition date deposition_date2018-08-29
Structure title titleCryo-EM structure of the PYD filament of AIM2
Keywords keywordsFilament, higher order, innate immunity, inflammasome, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.08
Radius of gyration Rg (electron density) rg_electron61.53
Forward intensity I(0) i04020290000.00
Molecular weight molecular_weight536370.0 kDa
Excluded volume excluded_volume670460 ų
Envelope volume envelope_volume1080100 ų
Hydration-shell volume shell_volume146100 ų
Envelope diameter envelope_diameter196.8
Shell Rg shell_rg64.58
Envelope Rg envelope_rg58.41
Shape Rg shape_rg61.60
Total Rg total_rg61.35
Total atoms total_atoms37650
Residues n_residues4725
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 dmax193.9
Rg (real space) rg_real61.68
Rg uncertainty (real space) rg_real_error1.70
I(0) (real space) i0_real4.0200e+09
I(0) uncertainty (real space) i0_real_error7.8070e+07
Rg (reciprocal space) rg_reciprocal62.40
I(0) (reciprocal space) i0_reciprocal4025000000.0000
Solution quality estimate total_estimate0.8570
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary77.6
Skewness Skewness skewness0.130
Kurtosis Kurtosis kurtosis-0.495
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha512100000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.935; Smooth: 0.514

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)