6k9f

Structure of unknow protein 4

Method: ELECTRON MICROSCOPY Dmax: 97.9 Å Quality: EXCELLENT

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 345–431 Chain B; UniProt 345–431 Chain C; UniProt 345–431 Chain D; UniProt 345–431 Chain E; UniProt 345–431 Chain F; UniProt 345–431 Chain G; UniProt 345–431 Chain H; UniProt 345–431 Chain I; UniProt 345–431 Chain J; UniProt 345–431 Chain K; UniProt 345–431 Chain L; UniProt 345–431 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 Å R-free 0.302

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
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–91; UniProt 345–431 Author chain B; PDBConstruct 5–91; UniProt 345–431 Author chain C; PDBConstruct 5–91; UniProt 345–431 Author chain D; PDBConstruct 5–91; UniProt 345–431 Author chain E; PDBConstruct 5–91; UniProt 345–431 Author chain F; PDBConstruct 5–91; UniProt 345–431 Author chain G; PDBConstruct 5–91; UniProt 345–431 Author chain H; PDBConstruct 5–91; UniProt 345–431 Author chain I; PDBConstruct 5–91; UniProt 345–431 Author chain J; PDBConstruct 5–91; UniProt 345–431 Author chain K; PDBConstruct 5–91; UniProt 345–431 Author chain L; PDBConstruct 5–91; UniProt 345–431

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 6k9f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6k9f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6k9f
Deposition date deposition_date2019-06-15
Structure title titleStructure of unknow protein 4
Keywords keywordsfilament, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.43
Radius of gyration Rg (electron density) rg_electron32.63
Forward intensity I(0) i0245069000.00
Molecular weight molecular_weight120820.0 kDa
Excluded volume excluded_volume150150 ų
Envelope volume envelope_volume213790 ų
Hydration-shell volume shell_volume53431 ų
Envelope diameter envelope_diameter103.8
Shell Rg shell_rg40.59
Envelope Rg envelope_rg31.68
Shape Rg shape_rg32.67
Total Rg total_rg33.18
Total atoms total_atoms8484
Residues n_residues1044
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 dmax97.9
Rg (real space) rg_real33.19
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.4510e+08
I(0) uncertainty (real space) i0_real_error3.0000e+06
Rg (reciprocal space) rg_reciprocal33.34
I(0) (reciprocal space) i0_reciprocal245100000.0000
Solution quality estimate total_estimate0.9007
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.8
Skewness Skewness skewness0.015
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha48980000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)