8fvu

Cryo-EM structure of human Needle/NAIP/NLRC4 (R288A)

Method: ELECTRON MICROSCOPY Dmax: 163.9 Å Quality: GOOD

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

Baculoviral IAP repeat-containing protein 1

Homo sapiens

UniProt Q13075

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–1403 Not recorded NLR family CARD domain-containing protein 4 × 1 (Q9NPP4) Lethal factor,Type III secretion system protein × 1 (P15917,Q63K18) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BIRC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–1409; UniProt 1–1403

NLR family CARD domain-containing protein 4

Homo sapiens

UniProt Q9NPP4

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–1024 Mutation:R288A Baculoviral IAP repeat-containing protein 1 × 1 (Q13075) Lethal factor,Type III secretion system protein × 1 (P15917,Q63K18) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

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

View Construct and Data Evidence
UniProt name NLRC4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 7–1030; UniProt 1–1024

Lethal factor,Type III secretion system protein

Burkholderia

UniProt P15917

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain U; UniProt 34–296 Not recorded Baculoviral IAP repeat-containing protein 1 × 1 (Q13075) NLR family CARD domain-containing protein 4 × 1 (Q9NPP4) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

30 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LEF_BACAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain U; PDBConstruct 21–283; UniProt 34–296

Lethal factor,Type III secretion system protein

Burkholderia

UniProt Q63K18

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 Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain U; UniProt 2–89 Not recorded Baculoviral IAP repeat-containing protein 1 × 1 (Q13075) NLR family CARD domain-containing protein 4 × 1 (Q9NPP4) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q63K18_BURPS
Isoform
PDB entities 3
Chains and sequence ranges Author chain U; PDBConstruct 287–374; UniProt 2–89

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 8fvu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8fvu
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8fvu
Deposition date deposition_date2023-01-19
Structure title titleCryo-EM structure of human Needle/NAIP/NLRC4 (R288A)
Keywords keywordsNLRC4, NAIP, 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_guinier50.07
Radius of gyration Rg (electron density) rg_electron49.78
Forward intensity I(0) i0992018000.00
Molecular weight molecular_weight266990.0 kDa
Excluded volume excluded_volume336140 ų
Envelope volume envelope_volume487030 ų
Hydration-shell volume shell_volume80692 ų
Envelope diameter envelope_diameter163.5
Shell Rg shell_rg54.91
Envelope Rg envelope_rg48.45
Shape Rg shape_rg49.77
Total Rg total_rg50.01
Total atoms total_atoms18758
Residues n_residues2344
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 dmax163.9
Rg (real space) rg_real50.00
Rg uncertainty (real space) rg_real_error1.77
I(0) (real space) i0_real9.9200e+08
I(0) uncertainty (real space) i0_real_error1.8120e+07
Rg (reciprocal space) rg_reciprocal50.11
I(0) (reciprocal space) i0_reciprocal992200000.0000
Solution quality estimate total_estimate0.8984
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary58.2
Skewness Skewness skewness0.200
Kurtosis Kurtosis kurtosis-0.606
Angular range angular_range— – 0.1550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha98330000.0000
Real-space data points n_real_points32
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.877

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)