9lez

Cryo-EM structure of human ZAC in complex with N-(4-(tert-butyl)thiazol-2-yl)-3-fluorobenzamide (TTFB)

Method: ELECTRON MICROSCOPY Dmax: 120.5 Å Quality: GOOD

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

Ligand-gated cation channel ZACN,Genome polyprotein

Enterovirus A71

UniProt B6F2F5

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 Homooligomer Protein × 5 其他Polymer 10 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 4–241 Chain B; UniProt 4–241 Chain C; UniProt 4–241 Chain D; UniProt 4–241 Chain E; UniProt 4–241 Mutation:A152T beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 A1EKJ ~{N}-(4-~{tert}-butyl-1,3-thiazol-2-yl)-3-fluoranyl-benzamide × 5 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

10 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B6F2F5_HE71
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 468–705; UniProt 4–241 Author chain B; PDBConstruct 468–705; UniProt 4–241 Author chain C; PDBConstruct 468–705; UniProt 4–241 Author chain D; PDBConstruct 468–705; UniProt 4–241 Author chain E; PDBConstruct 468–705; UniProt 4–241

Ligand-gated cation channel ZACN,Genome polyprotein

Enterovirus A71

UniProt Q401N2

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 Homooligomer Protein × 5 其他Polymer 10 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–412 Chain B; UniProt 1–412 Chain C; UniProt 1–412 Chain D; UniProt 1–412 Chain E; UniProt 1–412 Mutation:A152T beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 10 A1EKJ ~{N}-(4-~{tert}-butyl-1,3-thiazol-2-yl)-3-fluoranyl-benzamide × 5 ZN ZINC ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.54 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.

8 other PDB entries and 8 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ZACN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–412; UniProt 1–412 Author chain B; PDBConstruct 1–412; UniProt 1–412 Author chain C; PDBConstruct 1–412; UniProt 1–412 Author chain D; PDBConstruct 1–412; UniProt 1–412 Author chain E; PDBConstruct 1–412; UniProt 1–412

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 9lez

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9lez
Deposition date deposition_date2025-01-07
Structure title titleCryo-EM structure of human ZAC in complex with N-(4-(tert-butyl)thiazol-2-yl)-3-fluorobenzamide (TTFB)
Keywords keywordsCys-loop receptor, homopentamer, cation channel, TTFB binding state, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.35
Radius of gyration Rg (electron density) rg_electron36.73
Forward intensity I(0) i0913981000.00
Molecular weight molecular_weight169190.0 kDa
Excluded volume excluded_volume166120 ų
Envelope volume envelope_volume295600 ų
Hydration-shell volume shell_volume65079 ų
Envelope diameter envelope_diameter123.0
Shell Rg shell_rg44.61
Envelope Rg envelope_rg36.56
Shape Rg shape_rg36.73
Total Rg total_rg37.08
Total atoms total_atoms12840
Residues n_residues1555
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 dmax120.5
Rg (real space) rg_real37.26
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real9.1400e+08
I(0) uncertainty (real space) i0_real_error1.5870e+07
Rg (reciprocal space) rg_reciprocal37.32
I(0) (reciprocal space) i0_reciprocal914000000.0000
Solution quality estimate total_estimate0.8781
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.9
Skewness Skewness skewness0.325
Kurtosis Kurtosis kurtosis-0.302
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75750000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.849; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.876

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)