6ki0

Crystal Structure of Human ASC-CARD

Method: X-RAY DIFFRACTION Dmax: 123.5 Å Quality: GOOD

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

Maltose/maltodextrin-binding periplasmic protein,Apoptosis-associated speck-like protein containing a CARD

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–384 Fragment:caspase recruitment domain Mutation:D108A,K109A,E198A,N199A,K265A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291.15 K;1.80 M Ammonium Sulfate, 0.1 M HEPES 7.0 Resolution 2.00 Å R-free 0.252
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 27–384 Fragment:caspase recruitment domain Mutation:D108A,K109A,E198A,N199A,K265A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291.15 K;1.80 M Ammonium Sulfate, 0.1 M HEPES 7.0 Resolution 2.00 Å R-free 0.252

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.

366 other PDB entries and 490 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–359; UniProt 27–384 Author chain B; PDBConstruct 2–359; UniProt 27–384

Maltose/maltodextrin-binding periplasmic protein,Apoptosis-associated speck-like protein containing a CARD

Homo sapiens

UniProt Q9ULZ3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 112–195 Fragment:caspase recruitment domain Mutation:D108A,K109A,E198A,N199A,K265A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291.15 K;1.80 M Ammonium Sulfate, 0.1 M HEPES 7.0 Resolution 2.00 Å R-free 0.252
2 Insufficient information Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 112–195 Fragment:caspase recruitment domain Mutation:D108A,K109A,E198A,N199A,K265A alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;291.15 K;1.80 M Ammonium Sulfate, 0.1 M HEPES 7.0 Resolution 2.00 Å R-free 0.252

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.

17 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ASC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 372–455; UniProt 112–195 Author chain B; PDBConstruct 372–455; UniProt 112–195

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 6ki0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ki0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ki0
Deposition date deposition_date2019-07-16
Structure title titleCrystal Structure of Human ASC-CARD
Keywords keywordsDeath domain fold, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier35.14
Radius of gyration Rg (electron density) rg_electron35.14
Forward intensity I(0) i0151502000.00
Molecular weight molecular_weight102070.0 kDa
Excluded volume excluded_volume128870 ų
Envelope volume envelope_volume161650 ų
Hydration-shell volume shell_volume39258 ų
Envelope diameter envelope_diameter121.3
Shell Rg shell_rg40.54
Envelope Rg envelope_rg34.80
Shape Rg shape_rg35.15
Total Rg total_rg35.49
Total atoms total_atoms7210
Residues n_residues917
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 dmax123.5
Rg (real space) rg_real35.34
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real1.5150e+08
I(0) uncertainty (real space) i0_real_error2.9490e+06
Rg (reciprocal space) rg_reciprocal35.22
I(0) (reciprocal space) i0_reciprocal151500000.0000
Solution quality estimate total_estimate0.8411
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.9
Skewness Skewness skewness0.474
Kurtosis Kurtosis kurtosis-0.407
Angular range angular_range— – 0.2250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35140000.0000
Real-space data points n_real_points46
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.720; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.840; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6ki0A01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id6ki0B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)