8k39

Structure of the bacteriophage lambda portal vertex

Method: ELECTRON MICROSCOPY Dmax: 296.9 Å Quality: EXCELLENT

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

Major capsid protein

OrganismNot specified

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 0; UniProt 1–341 Chain 1; UniProt 1–341 Chain 2; UniProt 1–341 Chain 3; UniProt 1–341 Chain 4; UniProt 1–341 Chain 5; UniProt 1–341 Chain 6; UniProt 1–341 Chain 7; UniProt 1–341 Chain A; UniProt 1–341 Chain B; UniProt 1–341 Chain C; UniProt 1–341 Chain D; UniProt 1–341 Chain E; UniProt 1–341 Chain F; UniProt 1–341 Chain G; UniProt 1–341 Chain H; UniProt 1–341 Chain I; UniProt 1–341 Chain J; UniProt 1–341 Chain K; UniProt 1–341 Chain L; UniProt 1–341 Chain M; UniProt 1–341 Chain N; UniProt 1–341 Chain O; UniProt 1–341 Chain P; UniProt 1–341 Chain Q; UniProt 1–341 Chain R; UniProt 1–341 Chain S; UniProt 1–341 Chain T; UniProt 1–341 Chain g; UniProt 1–341 Chain h; UniProt 1–341 Not recorded Portal protein B × 12 (P03710) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 1
Chains and sequence ranges Author chain 0; PDBConstruct 1–341; UniProt 1–341 Author chain 1; PDBConstruct 1–341; UniProt 1–341 Author chain 2; PDBConstruct 1–341; UniProt 1–341 Author chain 3; PDBConstruct 1–341; UniProt 1–341 Author chain 4; PDBConstruct 1–341; UniProt 1–341 Author chain 5; PDBConstruct 1–341; UniProt 1–341 Author chain 6; PDBConstruct 1–341; UniProt 1–341 Author chain 7; PDBConstruct 1–341; UniProt 1–341 Author chain A; PDBConstruct 1–341; UniProt 1–341 Author chain B; PDBConstruct 1–341; UniProt 1–341 Author chain C; PDBConstruct 1–341; UniProt 1–341 Author chain D; PDBConstruct 1–341; UniProt 1–341 Author chain E; PDBConstruct 1–341; UniProt 1–341 Author chain F; PDBConstruct 1–341; UniProt 1–341 Author chain G; PDBConstruct 1–341; UniProt 1–341 Author chain H; PDBConstruct 1–341; UniProt 1–341 Author chain I; PDBConstruct 1–341; UniProt 1–341 Author chain J; PDBConstruct 1–341; UniProt 1–341 Author chain K; PDBConstruct 1–341; UniProt 1–341 Author chain L; PDBConstruct 1–341; UniProt 1–341 Author chain M; PDBConstruct 1–341; UniProt 1–341 Author chain N; PDBConstruct 1–341; UniProt 1–341 Author chain O; PDBConstruct 1–341; UniProt 1–341 Author chain P; PDBConstruct 1–341; UniProt 1–341 Author chain Q; PDBConstruct 1–341; UniProt 1–341 Author chain R; PDBConstruct 1–341; UniProt 1–341 Author chain S; PDBConstruct 1–341; UniProt 1–341 Author chain T; PDBConstruct 1–341; UniProt 1–341 Author chain g; PDBConstruct 1–341; UniProt 1–341 Author chain h; PDBConstruct 1–341; UniProt 1–341

Portal protein B

OrganismNot specified

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 U; UniProt 1–533 Chain V; UniProt 1–533 Chain W; UniProt 1–533 Chain X; UniProt 1–533 Chain Y; UniProt 1–533 Chain Z; UniProt 1–533 Chain a; UniProt 1–533 Chain b; UniProt 1–533 Chain c; UniProt 1–533 Chain d; UniProt 1–533 Chain e; UniProt 1–533 Chain f; UniProt 1–533 Not recorded Major capsid protein × 30 (P03713) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.00 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 2
Chains and sequence ranges Author chain U; PDBConstruct 1–533; UniProt 1–533 Author chain V; PDBConstruct 1–533; UniProt 1–533 Author chain W; PDBConstruct 1–533; UniProt 1–533 Author chain X; PDBConstruct 1–533; UniProt 1–533 Author chain Y; PDBConstruct 1–533; UniProt 1–533 Author chain Z; PDBConstruct 1–533; UniProt 1–533 Author chain a; PDBConstruct 1–533; UniProt 1–533 Author chain b; PDBConstruct 1–533; UniProt 1–533 Author chain c; PDBConstruct 1–533; UniProt 1–533 Author chain d; PDBConstruct 1–533; UniProt 1–533 Author chain e; PDBConstruct 1–533; UniProt 1–533 Author chain f; PDBConstruct 1–533; UniProt 1–533

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 8k39

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8k39
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8k39
Deposition date deposition_date2023-07-14
Structure title titleStructure of the bacteriophage lambda portal vertex
Keywords keywordsComplex, 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_electron107.60
Forward intensity I(0) i044810900000.00
Molecular weight molecular_weight1771900.0 kDa
Excluded volume excluded_volume2201400 ų
Envelope volume envelope_volume4199700 ų
Hydration-shell volume shell_volume324400 ų
Envelope diameter envelope_diameter364.0
Shell Rg shell_rg98.44
Envelope Rg envelope_rg108.10
Shape Rg shape_rg107.50
Total Rg total_rg107.60
Total atoms total_atoms124618
Residues n_residues15849
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 dmax296.9
Rg (real space) rg_real102.90
Rg uncertainty (real space) rg_real_error1.10
I(0) (real space) i0_real4.3000e+10
I(0) uncertainty (real space) i0_real_error9.9690e+08
Rg (reciprocal space) rg_reciprocal102.90
I(0) (reciprocal space) i0_reciprocal44230000000.0000
Solution quality estimate total_estimate0.9120
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary106.0
Skewness Skewness skewness0.300
Kurtosis Kurtosis kurtosis-0.548
Angular range angular_range— – 0.0700 −1
Current regularization parameter α current_alpha1.1630
Highest regularization parameter α highest_alpha2029000000.0000
Real-space data points n_real_points15
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.001; Oscil: 0.998; Stabil: 0.966; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)