8k38

The structure of bacteriophage lambda portal-adaptor

Method: ELECTRON MICROSCOPY Dmax: 172.8 Å Quality: GOOD

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

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count 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 Chain G; UniProt 1–533 Chain H; UniProt 1–533 Chain I; UniProt 1–533 Chain J; UniProt 1–533 Chain K; UniProt 1–533 Chain L; UniProt 1–533 Not recorded Head completion protein × 12 (P68660) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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 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 Author chain G; PDBConstruct 1–533; UniProt 1–533 Author chain H; PDBConstruct 1–533; UniProt 1–533 Author chain I; PDBConstruct 1–533; UniProt 1–533 Author chain J; PDBConstruct 1–533; UniProt 1–533 Author chain K; PDBConstruct 1–533; UniProt 1–533 Author chain L; PDBConstruct 1–533; UniProt 1–533

Head completion protein

OrganismNot specified

UniProt P68660

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 × 24 PDB declaration: 24-meric(24) Consistent with protein copy count Chain M; UniProt 1–68 Chain N; UniProt 1–68 Chain O; UniProt 1–68 Chain P; UniProt 1–68 Chain Q; UniProt 1–68 Chain R; UniProt 1–68 Chain S; UniProt 1–68 Chain T; UniProt 1–68 Chain U; UniProt 1–68 Chain V; UniProt 1–68 Chain W; UniProt 1–68 Chain X; UniProt 1–68 Not recorded Portal protein B × 12 (P03710) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HCP_LAMBD
Isoform
PDB entities 2
Chains and sequence ranges Author chain M; PDBConstruct 1–68; UniProt 1–68 Author chain N; PDBConstruct 1–68; UniProt 1–68 Author chain O; PDBConstruct 1–68; UniProt 1–68 Author chain P; PDBConstruct 1–68; UniProt 1–68 Author chain Q; PDBConstruct 1–68; UniProt 1–68 Author chain R; PDBConstruct 1–68; UniProt 1–68 Author chain S; PDBConstruct 1–68; UniProt 1–68 Author chain T; PDBConstruct 1–68; UniProt 1–68 Author chain U; PDBConstruct 1–68; UniProt 1–68 Author chain V; PDBConstruct 1–68; UniProt 1–68 Author chain W; PDBConstruct 1–68; UniProt 1–68 Author chain X; PDBConstruct 1–68; UniProt 1–68

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 8k38

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8k38
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8k38
Deposition date deposition_date2023-07-14
Structure title titleThe structure of bacteriophage lambda portal-adaptor
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_guinier57.16
Radius of gyration Rg (electron density) rg_electron56.39
Forward intensity I(0) i07742890000.00
Molecular weight molecular_weight713560.0 kDa
Excluded volume excluded_volume880200 ų
Envelope volume envelope_volume1258900 ų
Hydration-shell volume shell_volume170060 ų
Envelope diameter envelope_diameter168.3
Shell Rg shell_rg69.80
Envelope Rg envelope_rg55.42
Shape Rg shape_rg56.40
Total Rg total_rg56.63
Total atoms total_atoms50172
Residues n_residues6396
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 dmax172.8
Rg (real space) rg_real56.71
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real7.7430e+09
I(0) uncertainty (real space) i0_real_error1.4190e+08
Rg (reciprocal space) rg_reciprocal57.52
I(0) (reciprocal space) i0_reciprocal7752000000.0000
Solution quality estimate total_estimate0.8846
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary76.8
Skewness Skewness skewness-0.036
Kurtosis Kurtosis kurtosis-0.663
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1648000000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.795

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)