6xkj

Cryo-EM structure of CARD8-CARD filament

Method: ELECTRON MICROSCOPY Dmax: 110.7 Å Quality: GOOD

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

Caspase recruitment domain-containing protein 8

Homo sapiens

UniProt Q9Y2G2

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 451–537 Chain B; UniProt 451–537 Chain C; UniProt 451–537 Chain D; UniProt 451–537 Chain E; UniProt 451–537 Chain F; UniProt 451–537 Chain G; UniProt 451–537 Chain H; UniProt 451–537 Chain I; UniProt 451–537 Chain J; UniProt 451–537 Chain K; UniProt 451–537 Chain L; UniProt 451–537 Chain M; UniProt 451–537 Chain N; UniProt 451–537 Chain O; UniProt 451–537 Chain P; UniProt 451–537 Fragment:CARD domain (UNP residues 451-537) No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.54 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CARD8_HUMAN
Isoform Q9Y2G2-5
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–87; UniProt 451–537 Author chain B; PDBConstruct 1–87; UniProt 451–537 Author chain C; PDBConstruct 1–87; UniProt 451–537 Author chain D; PDBConstruct 1–87; UniProt 451–537 Author chain E; PDBConstruct 1–87; UniProt 451–537 Author chain F; PDBConstruct 1–87; UniProt 451–537 Author chain G; PDBConstruct 1–87; UniProt 451–537 Author chain H; PDBConstruct 1–87; UniProt 451–537 Author chain I; PDBConstruct 1–87; UniProt 451–537 Author chain J; PDBConstruct 1–87; UniProt 451–537 Author chain K; PDBConstruct 1–87; UniProt 451–537 Author chain L; PDBConstruct 1–87; UniProt 451–537 Author chain M; PDBConstruct 1–87; UniProt 451–537 Author chain N; PDBConstruct 1–87; UniProt 451–537 Author chain O; PDBConstruct 1–87; UniProt 451–537 Author chain P; PDBConstruct 1–87; UniProt 451–537

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 6xkj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6xkj
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id6xkj
Deposition date deposition_date2020-06-26
Structure title titleCryo-EM structure of CARD8-CARD filament
Keywords keywordsFilament, inflammasome, signaling, UPA, FIIND, CARD, NLRP1, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier35.43
Radius of gyration Rg (electron density) rg_electron34.77
Forward intensity I(0) i0404381000.00
Molecular weight molecular_weight157460.0 kDa
Excluded volume excluded_volume195600 ų
Envelope volume envelope_volume259750 ų
Hydration-shell volume shell_volume60749 ų
Envelope diameter envelope_diameter115.5
Shell Rg shell_rg42.75
Envelope Rg envelope_rg33.94
Shape Rg shape_rg34.81
Total Rg total_rg35.19
Total atoms total_atoms11056
Residues n_residues1360
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 dmax110.7
Rg (real space) rg_real35.23
Rg uncertainty (real space) rg_real_error0.73
I(0) (real space) i0_real4.0440e+08
I(0) uncertainty (real space) i0_real_error6.1650e+06
Rg (reciprocal space) rg_reciprocal35.36
I(0) (reciprocal space) i0_reciprocal404400000.0000
Solution quality estimate total_estimate0.8875
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.3
Skewness Skewness skewness0.173
Kurtosis Kurtosis kurtosis-0.375
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha83320000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.877; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)