8kge

Dimeric tail tube protein gpVs of bacteriophage lambda

Method: ELECTRON MICROSCOPY Dmax: 97.5 Å Quality: REASONABLE

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

Tail tube protein

Escherichia phage lambda

UniProt P03733

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain V; UniProt 1–246 Chain v; UniProt 1–246 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.80 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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TUBE_LAMBD
Isoform
PDB entities 1
Chains and sequence ranges Author chain V; PDBConstruct 1–246; UniProt 1–246 Author chain v; PDBConstruct 1–246; UniProt 1–246

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 8kge

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8kge
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8kge
Deposition date deposition_date2023-08-18
Structure title titleDimeric tail tube protein gpVs of bacteriophage lambda
Keywords keywordsBacteriophage, caudovirales, siphoviridae, tail complex, delivery device, phage lambda, cryo-EM, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier29.11
Radius of gyration Rg (electron density) rg_electron28.64
Forward intensity I(0) i044720400.00
Molecular weight molecular_weight50923.0 kDa
Excluded volume excluded_volume63379 ų
Envelope volume envelope_volume86978 ų
Hydration-shell volume shell_volume26915 ų
Envelope diameter envelope_diameter99.1
Shell Rg shell_rg33.64
Envelope Rg envelope_rg29.16
Shape Rg shape_rg28.63
Total Rg total_rg29.20
Total atoms total_atoms3584
Residues n_residues486
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 dmax97.5
Rg (real space) rg_real29.17
Rg uncertainty (real space) rg_real_error0.77
I(0) (real space) i0_real4.4720e+07
I(0) uncertainty (real space) i0_real_error6.2850e+05
Rg (reciprocal space) rg_reciprocal29.15
I(0) (reciprocal space) i0_reciprocal44720000.0000
Solution quality estimate total_estimate0.6367
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.7
Skewness Skewness skewness0.352
Kurtosis Kurtosis kurtosis-0.492
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6297000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 0.218; Positv: 1.000; Valcen: 0.942; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)