9rt2

NetF - ANTXR2 structure (C4)

Method: ELECTRON MICROSCOPY Dmax: 151.0 Å Quality: GOOD

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

Leukocidin/Hemolysin toxin family

Clostridium perfringens

UniProt A0A0D3QGV4

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 heterocomplex Heteromer Protein × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain N1; UniProt 25–305 Chain N2; UniProt 25–305 Chain N3; UniProt 25–305 Chain N4; UniProt 25–305 Chain N5; UniProt 25–305 Chain N6; UniProt 25–305 Chain N7; UniProt 25–305 Chain N8; UniProt 25–305 Not recorded Anthrax toxin receptor 2 × 4 (P58335) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0D3QGV4_CLOPF
Isoform
PDB entities 1
Chains and sequence ranges Author chain N1; PDBConstruct 9–289; UniProt 25–305 Author chain N2; PDBConstruct 9–289; UniProt 25–305 Author chain N3; PDBConstruct 9–289; UniProt 25–305 Author chain N4; PDBConstruct 9–289; UniProt 25–305 Author chain N5; PDBConstruct 9–289; UniProt 25–305 Author chain N6; PDBConstruct 9–289; UniProt 25–305 Author chain N7; PDBConstruct 9–289; UniProt 25–305 Author chain N8; PDBConstruct 9–289; UniProt 25–305

Anthrax toxin receptor 2

Homo sapiens

UniProt P58335

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 heterocomplex Heteromer Protein × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain C1; UniProt 34–318 Chain C2; UniProt 34–318 Chain C3; UniProt 34–318 Chain C4; UniProt 34–318 Mutation:deleted TM and cytoplasmic domains Leukocidin/Hemolysin toxin family × 8 (A0A0D3QGV4) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.60 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.

13 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ANTR2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C1; PDBConstruct 1–285; UniProt 34–318 Author chain C2; PDBConstruct 1–285; UniProt 34–318 Author chain C3; PDBConstruct 1–285; UniProt 34–318 Author chain C4; PDBConstruct 1–285; UniProt 34–318

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 9rt2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rt2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rt2
Deposition date deposition_date2025-07-01
Structure title titleNetF - ANTXR2 structure (C4)
Keywords keywordsNetF, clostridium perfringens, hemolysin, CMG2, ANTXR2, toxin receptor interaction, transmembrane beta-barrel, TOXIN; TOXIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.93
Radius of gyration Rg (electron density) rg_electron49.77
Forward intensity I(0) i01882030000.00
Molecular weight molecular_weight365170.0 kDa
Excluded volume excluded_volume458310 ų
Envelope volume envelope_volume641460 ų
Hydration-shell volume shell_volume106430 ų
Envelope diameter envelope_diameter160.7
Shell Rg shell_rg55.60
Envelope Rg envelope_rg47.87
Shape Rg shape_rg49.74
Total Rg total_rg50.07
Total atoms total_atoms51141
Residues n_residues3279
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 dmax151.0
Rg (real space) rg_real49.74
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real1.8820e+09
I(0) uncertainty (real space) i0_real_error3.0110e+07
Rg (reciprocal space) rg_reciprocal50.07
I(0) (reciprocal space) i0_reciprocal1883000000.0000
Solution quality estimate total_estimate0.8796
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary66.0
Skewness Skewness skewness0.134
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha143200000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.632

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)