8xqb

Mature virion portal vertex of bacteriophage lambda

Method: ELECTRON MICROSCOPY Dmax: 224.1 Å Quality: EXCELLENT

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 × 71 PDB declaration: 71-meric(71) 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) Major capsid protein × 15 (P03713) Capsid decoration protein × 20 (P03712) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 4.07 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 × 71 PDB declaration: 71-meric(71) 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) Major capsid protein × 15 (P03713) Capsid decoration protein × 20 (P03712) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 4.07 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 × 71 PDB declaration: 71-meric(71) 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) Major capsid protein × 15 (P03713) Capsid decoration protein × 20 (P03712) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 4.07 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 × 71 PDB declaration: 71-meric(71) 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) Major capsid protein × 15 (P03713) Capsid decoration protein × 20 (P03712) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 4.07 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

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 × 71 PDB declaration: 71-meric(71) 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 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 Head-tail connector protein FII × 6 (P03714) Head completion protein × 12 (P68660) Tail tube terminator protein × 6 (P03732) Portal protein B × 12 (P03710) Capsid decoration protein × 20 (P03712) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 4.07 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 5
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 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

Capsid decoration protein

OrganismNot specified

UniProt P03712

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 × 71 PDB declaration: 71-meric(71) Consistent with protein copy count Chain H0; UniProt 1–110 Chain H1; UniProt 1–110 Chain H2; UniProt 1–110 Chain H3; UniProt 1–110 Chain H4; UniProt 1–110 Chain I0; UniProt 1–110 Chain I1; UniProt 1–110 Chain I2; UniProt 1–110 Chain I3; UniProt 1–110 Chain I4; UniProt 1–110 Chain J0; UniProt 1–110 Chain J1; UniProt 1–110 Chain J2; UniProt 1–110 Chain J3; UniProt 1–110 Chain J4; UniProt 1–110 Chain N0; UniProt 1–110 Chain N1; UniProt 1–110 Chain N2; UniProt 1–110 Chain N3; UniProt 1–110 Chain N4; UniProt 1–110 Not recorded Head-tail connector protein FII × 6 (P03714) Head completion protein × 12 (P68660) Tail tube terminator protein × 6 (P03732) Portal protein B × 12 (P03710) Major capsid protein × 15 (P03713) ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen NITROGEN Resolution 4.07 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 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DECO_LAMBD
Isoform
PDB entities 6
Chains and sequence ranges Author chain H0; PDBConstruct 1–110; UniProt 1–110 Author chain H1; PDBConstruct 1–110; UniProt 1–110 Author chain H2; PDBConstruct 1–110; UniProt 1–110 Author chain H3; PDBConstruct 1–110; UniProt 1–110 Author chain H4; PDBConstruct 1–110; UniProt 1–110 Author chain I0; PDBConstruct 1–110; UniProt 1–110 Author chain I1; PDBConstruct 1–110; UniProt 1–110 Author chain I2; PDBConstruct 1–110; UniProt 1–110 Author chain I3; PDBConstruct 1–110; UniProt 1–110 Author chain I4; PDBConstruct 1–110; UniProt 1–110 Author chain J0; PDBConstruct 1–110; UniProt 1–110 Author chain J1; PDBConstruct 1–110; UniProt 1–110 Author chain J2; PDBConstruct 1–110; UniProt 1–110 Author chain J3; PDBConstruct 1–110; UniProt 1–110 Author chain J4; PDBConstruct 1–110; UniProt 1–110 Author chain N0; PDBConstruct 1–110; UniProt 1–110 Author chain N1; PDBConstruct 1–110; UniProt 1–110 Author chain N2; PDBConstruct 1–110; UniProt 1–110 Author chain N3; PDBConstruct 1–110; UniProt 1–110 Author chain N4; PDBConstruct 1–110; UniProt 1–110

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 8xqb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8xqb
Deposition date deposition_date2024-01-05
Structure title titleMature virion portal vertex of bacteriophage lambda
Keywords keywordscaudovirales, siphoviridae, 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_guinier85.36
Radius of gyration Rg (electron density) rg_electron85.40
Forward intensity I(0) i041003400000.00
Molecular weight molecular_weight1683600.0 kDa
Excluded volume excluded_volume2087400 ų
Envelope volume envelope_volume3303200 ų
Hydration-shell volume shell_volume305220 ų
Envelope diameter envelope_diameter311.0
Shell Rg shell_rg92.07
Envelope Rg envelope_rg86.23
Shape Rg shape_rg85.40
Total Rg total_rg85.45
Total atoms total_atoms118454
Residues n_residues15222
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 dmax224.1
Rg (real space) rg_real82.13
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real3.9070e+10
I(0) uncertainty (real space) i0_real_error6.0870e+08
Rg (reciprocal space) rg_reciprocal86.03
I(0) (reciprocal space) i0_reciprocal41080000000.0000
Solution quality estimate total_estimate0.9097
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary99.6
Skewness Skewness skewness0.128
Kurtosis Kurtosis kurtosis-0.573
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.9452
Highest regularization parameter α highest_alpha4697000000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.999; Stabil: 0.963; Sysdev: 1.000; Positv: 1.000; Valcen: 0.942; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)