8iyd

Tail cap of phage lambda tail

Method: ELECTRON MICROSCOPY Dmax: 249.2 Å Quality: GOOD

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 heterocomplex Heteromer Protein × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain A; UniProt 1–246 Chain B; UniProt 1–246 Chain C; UniProt 1–246 Chain D; UniProt 1–246 Chain E; UniProt 1–246 Chain F; UniProt 1–246 Chain H; UniProt 1–246 Chain I; UniProt 1–246 Chain J; UniProt 1–246 Chain L; UniProt 1–246 Chain M; UniProt 1–246 Chain N; UniProt 1–246 Chain O; UniProt 1–246 Chain P; UniProt 1–246 Chain R; UniProt 1–246 Chain S; UniProt 1–246 Chain T; UniProt 1–246 Chain V; UniProt 1–246 Chain X; UniProt 1–246 Chain Y; UniProt 1–246 Chain a; UniProt 1–246 Chain b; UniProt 1–246 Chain c; UniProt 1–246 Chain v; UniProt 1–246 Not recorded Tail tube terminator protein × 6 (P03732) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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 A; PDBConstruct 1–246; UniProt 1–246 Author chain B; PDBConstruct 1–246; UniProt 1–246 Author chain C; PDBConstruct 1–246; UniProt 1–246 Author chain D; PDBConstruct 1–246; UniProt 1–246 Author chain E; PDBConstruct 1–246; UniProt 1–246 Author chain F; PDBConstruct 1–246; UniProt 1–246 Author chain H; PDBConstruct 1–246; UniProt 1–246 Author chain I; PDBConstruct 1–246; UniProt 1–246 Author chain J; PDBConstruct 1–246; UniProt 1–246 Author chain L; PDBConstruct 1–246; UniProt 1–246 Author chain M; PDBConstruct 1–246; UniProt 1–246 Author chain N; PDBConstruct 1–246; UniProt 1–246 Author chain O; PDBConstruct 1–246; UniProt 1–246 Author chain P; PDBConstruct 1–246; UniProt 1–246 Author chain R; PDBConstruct 1–246; UniProt 1–246 Author chain S; PDBConstruct 1–246; UniProt 1–246 Author chain T; PDBConstruct 1–246; UniProt 1–246 Author chain V; PDBConstruct 1–246; UniProt 1–246 Author chain X; PDBConstruct 1–246; UniProt 1–246 Author chain Y; PDBConstruct 1–246; UniProt 1–246 Author chain a; PDBConstruct 1–246; UniProt 1–246 Author chain b; PDBConstruct 1–246; UniProt 1–246 Author chain c; PDBConstruct 1–246; UniProt 1–246 Author chain v; PDBConstruct 1–246; UniProt 1–246

Tail tube terminator protein

Escherichia phage lambda

UniProt P03732

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain G; UniProt 1–131 Chain K; UniProt 1–131 Chain Q; UniProt 1–131 Chain U; UniProt 1–131 Chain W; UniProt 1–131 Chain u; UniProt 1–131 Not recorded Tail tube protein × 24 (P03733) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.10 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.

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

View Construct and Data Evidence
UniProt name TTTP_LAMBD
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–131; UniProt 1–131 Author chain K; PDBConstruct 1–131; UniProt 1–131 Author chain Q; PDBConstruct 1–131; UniProt 1–131 Author chain U; PDBConstruct 1–131; UniProt 1–131 Author chain W; PDBConstruct 1–131; UniProt 1–131 Author chain u; PDBConstruct 1–131; UniProt 1–131

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 8iyd

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8iyd
Deposition date deposition_date2023-04-04
Structure title titleTail cap of phage lambda tail
Keywords keywords;Bacteriophage, caudovirales, siphoviridae, tail complex, delivery device, macromolecular assembly, 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_guinier69.77
Radius of gyration Rg (electron density) rg_electron69.75
Forward intensity I(0) i07071710000.00
Molecular weight molecular_weight700830.0 kDa
Excluded volume excluded_volume872480 ų
Envelope volume envelope_volume1462000 ų
Hydration-shell volume shell_volume175240 ų
Envelope diameter envelope_diameter223.6
Shell Rg shell_rg69.81
Envelope Rg envelope_rg66.92
Shape Rg shape_rg69.74
Total Rg total_rg69.77
Total atoms total_atoms49344
Residues n_residues6639
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 dmax249.2
Rg (real space) rg_real73.00
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real7.0900e+09
I(0) uncertainty (real space) i0_real_error1.3350e+08
Rg (reciprocal space) rg_reciprocal69.79
I(0) (reciprocal space) i0_reciprocal7072000000.0000
Solution quality estimate total_estimate0.8892
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.3
Skewness Skewness skewness0.535
Kurtosis Kurtosis kurtosis0.005
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha1.0850
Highest regularization parameter α highest_alpha1057000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 0.881; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.663

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)