8xou

Prohead portal vertex of bacteriophage lambda

Method: ELECTRON MICROSCOPY Dmax: 247.8 Å Quality: EXCELLENT

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

Portal protein B

Escherichia phage Lambda

UniProt P03710

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 × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain B; UniProt 1–533 Chain B1; UniProt 1–533 Chain B2; UniProt 1–533 Chain B3; UniProt 1–533 Chain B4; UniProt 1–533 Chain B5; UniProt 1–533 Chain b; UniProt 1–533 Chain b1; UniProt 1–533 Chain b2; UniProt 1–533 Chain b3; UniProt 1–533 Chain b4; UniProt 1–533 Chain b5; UniProt 1–533 Not recorded Major capsid protein × 30 (P03713) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 5.58 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PORTL_LAMBD
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–533; UniProt 1–533 Author chain B1; PDBConstruct 1–533; UniProt 1–533 Author chain B2; PDBConstruct 1–533; UniProt 1–533 Author chain B3; PDBConstruct 1–533; UniProt 1–533 Author chain B4; PDBConstruct 1–533; UniProt 1–533 Author chain B5; PDBConstruct 1–533; UniProt 1–533 Author chain b; PDBConstruct 1–533; UniProt 1–533 Author chain b1; PDBConstruct 1–533; UniProt 1–533 Author chain b2; PDBConstruct 1–533; UniProt 1–533 Author chain b3; PDBConstruct 1–533; UniProt 1–533 Author chain b4; PDBConstruct 1–533; UniProt 1–533 Author chain b5; PDBConstruct 1–533; UniProt 1–533

Major capsid protein

Escherichia phage Lambda

UniProt P03713

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 × 42 PDB declaration: 42-meric(42) Consistent with protein copy count Chain A0; UniProt 1–341 Chain A1; UniProt 1–341 Chain A2; UniProt 1–341 Chain A3; UniProt 1–341 Chain A4; UniProt 1–341 Chain C0; UniProt 1–341 Chain C1; UniProt 1–341 Chain C2; UniProt 1–341 Chain C3; UniProt 1–341 Chain C4; UniProt 1–341 Chain D0; UniProt 1–341 Chain D1; UniProt 1–341 Chain D2; UniProt 1–341 Chain D3; UniProt 1–341 Chain D4; UniProt 1–341 Chain E0; UniProt 1–341 Chain E1; UniProt 1–341 Chain E2; UniProt 1–341 Chain E3; UniProt 1–341 Chain E4; UniProt 1–341 Chain F0; UniProt 1–341 Chain F1; UniProt 1–341 Chain F2; UniProt 1–341 Chain F3; UniProt 1–341 Chain F4; UniProt 1–341 Chain G0; UniProt 1–341 Chain G1; UniProt 1–341 Chain G2; UniProt 1–341 Chain G3; UniProt 1–341 Chain G4; UniProt 1–341 Not recorded Portal protein B × 12 (P03710) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 5.58 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 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPSD_LAMBD
Isoform
PDB entities 2
Chains and sequence ranges Author chain A0; PDBConstruct 1–341; UniProt 1–341 Author chain A1; PDBConstruct 1–341; UniProt 1–341 Author chain A2; PDBConstruct 1–341; UniProt 1–341 Author chain A3; PDBConstruct 1–341; UniProt 1–341 Author chain A4; PDBConstruct 1–341; UniProt 1–341 Author chain C0; PDBConstruct 1–341; UniProt 1–341 Author chain C1; PDBConstruct 1–341; UniProt 1–341 Author chain C2; PDBConstruct 1–341; UniProt 1–341 Author chain C3; PDBConstruct 1–341; UniProt 1–341 Author chain C4; PDBConstruct 1–341; UniProt 1–341 Author chain D0; PDBConstruct 1–341; UniProt 1–341 Author chain D1; PDBConstruct 1–341; UniProt 1–341 Author chain D2; PDBConstruct 1–341; UniProt 1–341 Author chain D3; PDBConstruct 1–341; UniProt 1–341 Author chain D4; PDBConstruct 1–341; UniProt 1–341 Author chain E0; PDBConstruct 1–341; UniProt 1–341 Author chain E1; PDBConstruct 1–341; UniProt 1–341 Author chain E2; PDBConstruct 1–341; UniProt 1–341 Author chain E3; PDBConstruct 1–341; UniProt 1–341 Author chain E4; PDBConstruct 1–341; UniProt 1–341 Author chain F0; PDBConstruct 1–341; UniProt 1–341 Author chain F1; PDBConstruct 1–341; UniProt 1–341 Author chain F2; PDBConstruct 1–341; UniProt 1–341 Author chain F3; PDBConstruct 1–341; UniProt 1–341 Author chain F4; PDBConstruct 1–341; UniProt 1–341 Author chain G0; PDBConstruct 1–341; UniProt 1–341 Author chain G1; PDBConstruct 1–341; UniProt 1–341 Author chain G2; PDBConstruct 1–341; UniProt 1–341 Author chain G3; PDBConstruct 1–341; UniProt 1–341 Author chain G4; PDBConstruct 1–341; UniProt 1–341

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 8xou

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8xou
Deposition date deposition_date2024-01-02
Structure title titleProhead portal vertex of bacteriophage lambda
Keywords keywords;caudovirales, siphoviridae, portal vertex, portal, capsid, connector/neck, tail, delivery device, B-DNA, phage lambda, VIRAL PROTEIN ;; VIRAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier91.90
Radius of gyration Rg (electron density) rg_electron92.18
Forward intensity I(0) i044055600000.00
Molecular weight molecular_weight1756500.0 kDa
Excluded volume excluded_volume2182700 ų
Envelope volume envelope_volume3631300 ų
Hydration-shell volume shell_volume318640 ų
Envelope diameter envelope_diameter291.3
Shell Rg shell_rg94.71
Envelope Rg envelope_rg90.13
Shape Rg shape_rg92.17
Total Rg total_rg92.21
Total atoms total_atoms123582
Residues n_residues15738
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 dmax247.8
Rg (real space) rg_real89.15
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real4.2230e+10
I(0) uncertainty (real space) i0_real_error7.1530e+08
Rg (reciprocal space) rg_reciprocal91.89
I(0) (reciprocal space) i0_reciprocal44050000000.0000
Solution quality estimate total_estimate0.9076
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary102.0
Skewness Skewness skewness0.252
Kurtosis Kurtosis kurtosis-0.493
Angular range angular_range— – 0.0850 −1
Current regularization parameter α current_alpha0.9439
Highest regularization parameter α highest_alpha3509000000.0000
Real-space data points n_real_points18
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.985; Stabil: 0.948; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.001

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)