9ze4

Asymmetric Tail Gating Complex of Pseudomonas Phage DEV

Method: ELECTRON MICROSCOPY Dmax: 305.7 Å Quality: GOOD

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

gp75 tail tube

OrganismNot specified

UniProt A0A2K8I3N9

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 1–321 Chain B; UniProt 1–321 Chain C; UniProt 1–321 Chain D; UniProt 1–321 Chain E; UniProt 1–321 Chain F; UniProt 1–321 Chain G; UniProt 1–321 Chain H; UniProt 1–321 Chain I; UniProt 1–321 Chain J; UniProt 1–321 Chain K; UniProt 1–321 Chain L; UniProt 1–321 Not recorded N4 gp53-like protein × 1 (A0A2K8HNE9) Tip attachment protein J central straight fiber domain-containing protein × 3 (A0A2K8HW65) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.50 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2K8I3N9_9CAUD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–321; UniProt 1–321 Author chain B; PDBConstruct 1–321; UniProt 1–321 Author chain C; PDBConstruct 1–321; UniProt 1–321 Author chain D; PDBConstruct 1–321; UniProt 1–321 Author chain E; PDBConstruct 1–321; UniProt 1–321 Author chain F; PDBConstruct 1–321; UniProt 1–321 Author chain G; PDBConstruct 1–321; UniProt 1–321 Author chain H; PDBConstruct 1–321; UniProt 1–321 Author chain I; PDBConstruct 1–321; UniProt 1–321 Author chain J; PDBConstruct 1–321; UniProt 1–321 Author chain K; PDBConstruct 1–321; UniProt 1–321 Author chain L; PDBConstruct 1–321; UniProt 1–321

N4 gp53-like protein

OrganismNot specified

UniProt A0A2K8HNE9

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain M; UniProt 1–740 Not recorded gp75 tail tube × 12 (A0A2K8I3N9) Tip attachment protein J central straight fiber domain-containing protein × 3 (A0A2K8HW65) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.50 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 A0A2K8HNE9_9CAUD
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 1–740; UniProt 1–740

Tip attachment protein J central straight fiber domain-containing protein

OrganismNot specified

UniProt A0A2K8HW65

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 × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain N; UniProt 1–429 Chain O; UniProt 1–429 Chain P; UniProt 1–429 Not recorded gp75 tail tube × 12 (A0A2K8I3N9) N4 gp53-like protein × 1 (A0A2K8HNE9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 8.50 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 A0A2K8HW65_9CAUD
Isoform
PDB entities 3
Chains and sequence ranges Author chain N; PDBConstruct 1–429; UniProt 1–429 Author chain O; PDBConstruct 1–429; UniProt 1–429 Author chain P; PDBConstruct 1–429; UniProt 1–429

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 9ze4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ze4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ze4
Deposition date deposition_date2025-11-27
Structure title titleAsymmetric Tail Gating Complex of Pseudomonas Phage DEV
Keywords keywordsvirus, bacteriophage, receptor-binding protein, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron119.30
Forward intensity I(0) i03815300000.00
Molecular weight molecular_weight509720.0 kDa
Excluded volume excluded_volume633890 ų
Envelope volume envelope_volume1145300 ų
Hydration-shell volume shell_volume106920 ų
Envelope diameter envelope_diameter428.9
Shell Rg shell_rg61.55
Envelope Rg envelope_rg117.10
Shape Rg shape_rg119.40
Total Rg total_rg118.20
Total atoms total_atoms35853
Residues n_residues4951
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 dmax305.7
Rg (real space) rg_real105.80
Rg uncertainty (real space) rg_real_error2.37
I(0) (real space) i0_real3.6540e+09
I(0) uncertainty (real space) i0_real_error8.6090e+07
Rg (reciprocal space) rg_reciprocal92.24
I(0) (reciprocal space) i0_reciprocal3560000000.0000
Solution quality estimate total_estimate0.8330
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary70.5
Skewness Skewness skewness0.456
Kurtosis Kurtosis kurtosis-0.940
Angular range angular_range— – 0.0650 −1
Current regularization parameter α current_alpha0.1404
Highest regularization parameter α highest_alpha80630000.0000
Real-space data points n_real_points14
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.015; Oscil: 0.564; Stabil: 0.958; Sysdev: 1.000; Positv: 1.000; Valcen: 0.838; Smooth: 0.430

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)