SAXSdb — 8fw9

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

NLR family CARD domain-containing protein 4

Homo sapiens

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 × 3 PDB declaration: trimeric（3） Consistent with protein copy count	Chain A； UniProt 1–1024 Chain B； UniProt 1–1024 Chain C； UniProt 1–1024	Not recorded	No other associated polymer	ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5 cryo-EM vitrification conditions：Cryogen ETHANE	Resolution 4.46 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.

Other PDB	Difference from Current Entry 8FW9	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
6K8J Structure of NLRC4 CARD filament Deposited 2019-06-12	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 12 PDB declaration: dodecameric	Chain A 1–85（85 aa） Chain B 1–85（85 aa） Chain C 1–85（85 aa） Chain D 1–85（85 aa） Chain E 1–85（85 aa） Chain F 1–85（85 aa） Chain G 1–85（85 aa） Chain H 1–85（85 aa） Chain I 1–85（85 aa） Chain J 1–85（85 aa） Chain K 1–85（85 aa） Chain L 1–85（85 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.30 Å R-free 0.306
6MKS Cryo-EM structure of NLRC4-CARD filament Deposited 2018-09-26	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Insufficient information Homooligomer；Protein × 31 PDB declaration: 31-meric	Chain A 1–96（96 aa） Chain B 1–96（96 aa） Chain C 1–96（96 aa） Chain D 1–96（96 aa） Chain E 1–96（96 aa） Chain F 1–96（96 aa） Chain G 1–96（96 aa） Chain H 1–96（96 aa） Chain I 1–96（96 aa） Chain J 1–96（96 aa） Chain K 1–96（96 aa） Chain L 1–96（96 aa） Chain M 1–96（96 aa） Chain N 1–96（96 aa） Chain O 1–96（96 aa） Chain P 1–96（96 aa） Chain Q 1–96（96 aa） Chain R 1–96（96 aa） Chain S 1–96（96 aa） Chain T 1–96（96 aa） Chain U 1–96（96 aa） Chain V 1–96（96 aa） Chain W 1–96（96 aa） Chain X 1–96（96 aa） Chain Y 1–96（96 aa） Chain Z 1–96（96 aa） Chain a 1–96（96 aa） Chain b 1–96（96 aa） Chain c 1–96（96 aa） Chain d 1–96（96 aa） Chain e 1–96（96 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7；20mM HEPES at pH 7.4, 400mM NaCl, 10% glycerol, 1mM EDTA and 1mM DTT cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
6N1I Cryo-EM structure of NLRC4-CARD filament Deposited 2018-11-08	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric	Chain A 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain B 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain C 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain D 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain E 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain F 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain G 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain H 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain I 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain J 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain K 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain L 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain M 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain N 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain O 1–85（85 aa） Fragment：CARD (UNP residues 1-85) Chain P 1–85（85 aa） Fragment：CARD (UNP residues 1-85)	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.58 Å
8FVU Cryo-EM structure of human Needle/NAIP/NLRC4 (R288A) Deposited 2023-01-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric	Chain B 1–1024（1024 aa）	Mutation：R288A	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
8FW2 Cryo-EM structure of full-length human NLRC4 inflammasome with C11 symmetry Deposited 2023-01-20	Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric	Chain A 1–1024（1024 aa） Chain B 1–1024（1024 aa） Chain C 1–1024（1024 aa）	Not recorded	No recorded non-water small molecule	ELECTRON MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.80 Å

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	1
Chains and sequence ranges	Author chain A； PDBConstruct 7–1030； UniProt 1–1024 Author chain B； PDBConstruct 7–1030； UniProt 1–1024 Author chain C； PDBConstruct 7–1030； UniProt 1–1024

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	8fw9
Deposition date deposition_date	2023-01-20
Structure title title	Cryo-EM structure of full-length human NLRC4 inflammasome with C12 symmetry
Keywords keywords	NLRC4, NAIP, Inflammasome, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method method	ELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier	59.68 Å
Radius of gyration Rg (electron density) rg_electron	59.89 Å
Forward intensity I(0) i0	1266320000.00
Molecular weight molecular_weight	307240.0 kDa
Excluded volume excluded_volume	388510 Å³
Envelope volume envelope_volume	591150 Å³
Hydration-shell volume shell_volume	86074 Å³
Envelope diameter envelope_diameter	205.1 Å
Shell Rg shell_rg	58.02 Å
Envelope Rg envelope_rg	58.02 Å
Shape Rg shape_rg	59.85 Å
Total Rg total_rg	59.98 Å
Total atoms total_atoms	21612
Residues n_residues	2712
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	210.3 Å
Rg (real space) rg_real	59.92 Å
Rg uncertainty (real space) rg_real_error	2.56 Å
I(0) (real space) i0_real	1.2660e+09
I(0) uncertainty (real space) i0_real_error	2.6070e+07
Rg (reciprocal space) rg_reciprocal	59.46 Å
I(0) (reciprocal space) i0_reciprocal	1265000000.0000
Solution quality estimate total_estimate	0.8584
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	72.8 Å
Skewness Skewness skewness	0.393
Kurtosis Kurtosis kurtosis	-0.320
Angular range angular_range	— – 0.1300 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	66640000.0000
Real-space data points n_real_points	27
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.626

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Description description	NLR family CARD domain-containing protein 4
Molecular weight formula_weight	117027.7 kDa
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	21612

AEYCFNMNFIKDNSRALIQRMGMTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPLFQDLNGQSLFHQTSEGDLDDLAQDLKDLYHTPSFLNFYPLGEDIDIIFNLKSTFTEPVLWRKDQHHHRVEQLTLNGLLQALQSPCIIEGESGKGKSTLLQRIAMLWGSGKCKALTKFKFVFFLRLSRAQGGLFETLCDQLLDIPGTIRKQTFMAMLLKLRQRVLFLLDGYNEFKPQNCPEIEALIKENHRFKNMVIVTTTTECLRHIRQFGALTAEVGDMTEDSAQALIREVLIKELAEGLLLQIQKSRCLRNLMKTPLFVVITCAIQMGESEFHSHTQTTLFHTFYDLLIQKNKHKHKGVAASDFIRSLDHCGDLALEGVFSHKFDFELQDVSSVNEDVLLTTGLLCKYTAQRFKPKYKFFHKSFQEYTAGRRLSSLLTSHEPEEVTKGNGYLQKMVSISDITSTYSSLLRYTCGSSVEATRAVMKHLAAVYQHGCLLGLSIAKRPLWRQESLQSVKNTTEQEILKAININSFVECGIHLYQESTSKSALSQEFEAFFQGKSLYINSGNIPDYLFDFFEHLPNCASALDFIKLDFYGGAMASWEKAAEDTGGIHMEEAPETYIPSRAVSLFFNWKQEFRTLEVTLRDFSKLNKQDIRYLGKIFSSATSLRLQIKRCAGVAGSLSLVLSTCKNIYSLMVEASPLTIEDERHITSVTNLKTLSIHDLQNQRLPGGLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKMCLFHLTHLSDIGEGMDYIVKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEALHELIDRMNVLEQLTALMLPWGCDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQLNLAGNRVSSDGWLAFMGVFENLKQLVFFDFSTKEFLPDPALVRKLSQVLSKLTFLQEARLVGWQFDDDDLSVITGAFKLVTA

来源 Source

来源生物 organism	Homo sapiens
通用名 common_name	human
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	Spodoptera frugiperda

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8. Citations (1)

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Unit-cell length a length_a	1.000 Å
Unit-cell length b length_b	1.000 Å
Unit-cell length c length_c	1.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	—

Space group space_group	P 1
Space-group number int_tables_number	1
Crystal system crystal_system	—

Resolution resolution	4.46 Å
Resolution测定方法 resolution_method	—
颗粒数 num_particles	21406

fit	/app/data/saxs_computation/fw/8fw9/8fw9.fit
pddf	/app/data/pr_computation/fw/8fw9/8fw9.pr.out
profile	/app/data/saxs_computation/fw/8fw9/8fw9.dat

Cryo-EM structure of full-length human NLRC4 inflammasome with C12 symmetry

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

NLR family CARD domain-containing protein 4

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

冷冻电镜 EM 3D

6. Entities and Polymers Entities & Polymers (1)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)