9yft

N4 Bacteriophage Asymmetric Tail Gating Complex

Method: ELECTRON MICROSCOPY Dmax: 133.1 Å Quality: REASONABLE

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

Gp53

OrganismNot specified

UniProt Q859Q2

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain FA; UniProt 1–885 Not recorded Non-contractile tail sheath × 1 (A0MZE7) Gp54 × 12 (Q859Q3) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.61 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q859Q2_BPN4
Isoform
PDB entities 1
Chains and sequence ranges Author chain FA; PDBConstruct 1–885; UniProt 1–885

Non-contractile tail sheath

OrganismNot specified

UniProt A0MZE7

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain LA; UniProt 1–1382 Not recorded Gp53 × 1 (Q859Q2) Gp54 × 12 (Q859Q3) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.61 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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCTSP_BPN4
Isoform
PDB entities 2
Chains and sequence ranges Author chain LA; PDBConstruct 1–1382; UniProt 1–1382

Gp54

OrganismNot specified

UniProt Q859Q3

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain TA; UniProt 1–299 Chain TB; UniProt 1–299 Chain TC; UniProt 1–299 Chain TD; UniProt 1–299 Chain TE; UniProt 1–299 Chain TF; UniProt 1–299 Chain TG; UniProt 1–299 Chain TH; UniProt 1–299 Chain TI; UniProt 1–299 Chain TJ; UniProt 1–299 Chain TK; UniProt 1–299 Chain TL; UniProt 1–299 Not recorded Gp53 × 1 (Q859Q2) Non-contractile tail sheath × 1 (A0MZE7) ELECTRON MICROSCOPY mmCIF provides none of the parsed experimental conditions Resolution 3.61 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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q859Q3_BPN4
Isoform
PDB entities 3
Chains and sequence ranges Author chain TA; PDBConstruct 1–299; UniProt 1–299 Author chain TB; PDBConstruct 1–299; UniProt 1–299 Author chain TC; PDBConstruct 1–299; UniProt 1–299 Author chain TD; PDBConstruct 1–299; UniProt 1–299 Author chain TE; PDBConstruct 1–299; UniProt 1–299 Author chain TF; PDBConstruct 1–299; UniProt 1–299 Author chain TG; PDBConstruct 1–299; UniProt 1–299 Author chain TH; PDBConstruct 1–299; UniProt 1–299 Author chain TI; PDBConstruct 1–299; UniProt 1–299 Author chain TJ; PDBConstruct 1–299; UniProt 1–299 Author chain TK; PDBConstruct 1–299; UniProt 1–299 Author chain TL; PDBConstruct 1–299; UniProt 1–299

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 9yft

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9yft
Deposition date deposition_date2025-09-26
Structure title titleN4 Bacteriophage Asymmetric Tail Gating Complex
Keywords keywordsbacteriophage, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.70
Radius of gyration Rg (electron density) rg_electron51.32
Forward intensity I(0) i0599545000.00
Molecular weight molecular_weight200940.0 kDa
Excluded volume excluded_volume251160 ų
Envelope volume envelope_volume362150 ų
Hydration-shell volume shell_volume66613 ų
Envelope diameter envelope_diameter230.0
Shell Rg shell_rg47.71
Envelope Rg envelope_rg54.49
Shape Rg shape_rg51.31
Total Rg total_rg51.21
Total atoms total_atoms14173
Residues n_residues1832
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 dmax133.1
Rg (real space) rg_real44.28
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real5.6800e+08
I(0) uncertainty (real space) i0_real_error8.2500e+06
Rg (reciprocal space) rg_reciprocal49.71
I(0) (reciprocal space) i0_reciprocal597800000.0000
Solution quality estimate total_estimate0.7231
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.9
Skewness Skewness skewness0.482
Kurtosis Kurtosis kurtosis-0.196
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.1040
Highest regularization parameter α highest_alpha60650000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.010; Oscil: 0.898; Stabil: 0.989; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.784

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)