8xow

Mature virion portal of bacteriophage lambda

Method: ELECTRON MICROSCOPY Dmax: 205.1 Å Quality: GOOD

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

Head-tail connector protein FII

OrganismNot specified

UniProt P03714

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain f; UniProt 1–117 Chain f1; UniProt 1–117 Chain f2; UniProt 1–117 Chain f3; UniProt 1–117 Chain f4; UniProt 1–117 Chain f5; UniProt 1–117 Not recorded Head completion protein × 12 (P68660) Tail tube terminator protein × 6 (P03732) Portal protein B × 12 (P03710) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.32 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FII_LAMBD
Isoform
PDB entities 1
Chains and sequence ranges Author chain f; PDBConstruct 1–117; UniProt 1–117 Author chain f1; PDBConstruct 1–117; UniProt 1–117 Author chain f2; PDBConstruct 1–117; UniProt 1–117 Author chain f3; PDBConstruct 1–117; UniProt 1–117 Author chain f4; PDBConstruct 1–117; UniProt 1–117 Author chain f5; PDBConstruct 1–117; UniProt 1–117

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain W; UniProt 1–68 Chain W1; UniProt 1–68 Chain W2; UniProt 1–68 Chain W3; UniProt 1–68 Chain W4; UniProt 1–68 Chain W5; UniProt 1–68 Chain w; UniProt 1–68 Chain w1; UniProt 1–68 Chain w2; UniProt 1–68 Chain w3; UniProt 1–68 Chain w4; UniProt 1–68 Chain w5; UniProt 1–68 Not recorded Head-tail connector protein FII × 6 (P03714) Tail tube terminator protein × 6 (P03732) Portal protein B × 12 (P03710) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.32 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 W; PDBConstruct 1–68; UniProt 1–68 Author chain W1; PDBConstruct 1–68; UniProt 1–68 Author chain W2; PDBConstruct 1–68; UniProt 1–68 Author chain W3; PDBConstruct 1–68; UniProt 1–68 Author chain W4; PDBConstruct 1–68; UniProt 1–68 Author chain W5; PDBConstruct 1–68; UniProt 1–68 Author chain w; PDBConstruct 1–68; UniProt 1–68 Author chain w1; PDBConstruct 1–68; UniProt 1–68 Author chain w2; PDBConstruct 1–68; UniProt 1–68 Author chain w3; PDBConstruct 1–68; UniProt 1–68 Author chain w4; PDBConstruct 1–68; UniProt 1–68 Author chain w5; PDBConstruct 1–68; UniProt 1–68

Tail tube terminator protein

OrganismNot specified

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 × 36 PDB declaration: 36-meric(36) Consistent with protein copy count Chain U; UniProt 1–131 Chain U1; UniProt 1–131 Chain U2; UniProt 1–131 Chain U3; UniProt 1–131 Chain U4; UniProt 1–131 Chain U5; UniProt 1–131 Not recorded Head-tail connector protein FII × 6 (P03714) Head completion protein × 12 (P68660) Portal protein B × 12 (P03710) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.32 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 3
Chains and sequence ranges Author chain U; PDBConstruct 1–131; UniProt 1–131 Author chain U1; PDBConstruct 1–131; UniProt 1–131 Author chain U2; PDBConstruct 1–131; UniProt 1–131 Author chain U3; PDBConstruct 1–131; UniProt 1–131 Author chain U4; PDBConstruct 1–131; UniProt 1–131 Author chain U5; PDBConstruct 1–131; UniProt 1–131

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 × 36 PDB declaration: 36-meric(36) 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 Head-tail connector protein FII × 6 (P03714) Head completion protein × 12 (P68660) Tail tube terminator protein × 6 (P03732) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 3.32 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 4
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

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 8xow

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8xow
Deposition date deposition_date2024-01-02
Structure title titleMature virion portal 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_guinier68.38
Radius of gyration Rg (electron density) rg_electron68.49
Forward intensity I(0) i011871400000.00
Molecular weight molecular_weight886080.0 kDa
Excluded volume excluded_volume1092500 ų
Envelope volume envelope_volume1544400 ų
Hydration-shell volume shell_volume185350 ų
Envelope diameter envelope_diameter223.5
Shell Rg shell_rg71.88
Envelope Rg envelope_rg67.43
Shape Rg shape_rg68.53
Total Rg total_rg68.38
Total atoms total_atoms62334
Residues n_residues7962
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 dmax205.1
Rg (real space) rg_real68.39
Rg uncertainty (real space) rg_real_error1.20
I(0) (real space) i0_real1.1870e+10
I(0) uncertainty (real space) i0_real_error2.3040e+08
Rg (reciprocal space) rg_reciprocal68.19
I(0) (reciprocal space) i0_reciprocal11870000000.0000
Solution quality estimate total_estimate0.8364
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary80.3
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.359
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0004
Highest regularization parameter α highest_alpha1845000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.958; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.010

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)