6p2a

Chimera of bacteriophage OBP gp146 central spike protein and a T4 gp5 beta-helix fragment

Method: X-RAY DIFFRACTION Dmax: 151.3 Å Quality: REASONABLE

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

CHIMERA OF BACTERIOPHAGE OBP GP146 AND A T4 GP5

Pseudomonas phage OBP

UniProt G9IA38

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 259–326 Chain B; UniProt 259–326 Chain C; UniProt 259–326 Not recorded FE2 FE (II) ION × 1 STE STEARIC ACID × 1 ELA Elaidic acid × 1 PLM PALMITIC ACID × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;PEG3350 18-20% 100 mM Ammonium citrate Resolution 1.90 Å R-free 0.158
2 Insufficient information Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 259–326 Chain E; UniProt 259–326 Chain F; UniProt 259–326 Not recorded FE2 FE (II) ION × 1 STE STEARIC ACID × 1 ELA Elaidic acid × 1 PLM PALMITIC ACID × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;PEG3350 18-20% 100 mM Ammonium citrate Resolution 1.90 Å R-free 0.158

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name G9IA38_9CAUD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 81–148; UniProt 259–326 Author chain B; PDBConstruct 81–148; UniProt 259–326 Author chain C; PDBConstruct 81–148; UniProt 259–326 Author chain D; PDBConstruct 81–148; UniProt 259–326 Author chain E; PDBConstruct 81–148; UniProt 259–326 Author chain F; PDBConstruct 81–148; UniProt 259–326

CHIMERA OF BACTERIOPHAGE OBP GP146 AND A T4 GP5

Pseudomonas phage OBP

UniProt P16009

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 484–559 Chain B; UniProt 484–559 Chain C; UniProt 484–559 Not recorded FE2 FE (II) ION × 1 STE STEARIC ACID × 1 ELA Elaidic acid × 1 PLM PALMITIC ACID × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;PEG3350 18-20% 100 mM Ammonium citrate Resolution 1.90 Å R-free 0.158
2 Insufficient information Homooligomer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 484–559 Chain E; UniProt 484–559 Chain F; UniProt 484–559 Not recorded FE2 FE (II) ION × 1 STE STEARIC ACID × 1 ELA Elaidic acid × 1 PLM PALMITIC ACID × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;293 K;PEG3350 18-20% 100 mM Ammonium citrate Resolution 1.90 Å R-free 0.158

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.

17 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name BP5_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–80; UniProt 484–559 Author chain B; PDBConstruct 5–80; UniProt 484–559 Author chain C; PDBConstruct 5–80; UniProt 484–559 Author chain D; PDBConstruct 5–80; UniProt 484–559 Author chain E; PDBConstruct 5–80; UniProt 484–559 Author chain F; PDBConstruct 5–80; UniProt 484–559

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 6p2a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6p2a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6p2a
Deposition date deposition_date2019-05-21
Structure title titleChimera of bacteriophage OBP gp146 central spike protein and a T4 gp5 beta-helix fragment
Keywords keywords;Bacteriophage OBP, membrane piercing, central spike, cell puncturing device, beta helix, T4 gp5, contractile injection system, viral protein ;; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.56
Radius of gyration Rg (electron density) rg_electron37.51
Forward intensity I(0) i0146491000.00
Molecular weight molecular_weight91679.0 kDa
Excluded volume excluded_volume112420 ų
Envelope volume envelope_volume140910 ų
Hydration-shell volume shell_volume35869 ų
Envelope diameter envelope_diameter159.5
Shell Rg shell_rg37.51
Envelope Rg envelope_rg37.60
Shape Rg shape_rg37.51
Total Rg total_rg37.50
Total atoms total_atoms12606
Residues n_residues871
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 dmax151.3
Rg (real space) rg_real38.32
Rg uncertainty (real space) rg_real_error2.17
I(0) (real space) i0_real1.4650e+08
I(0) uncertainty (real space) i0_real_error2.9100e+06
Rg (reciprocal space) rg_reciprocal37.84
I(0) (reciprocal space) i0_reciprocal146400000.0000
Solution quality estimate total_estimate0.7351
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.6
Skewness Skewness skewness0.821
Kurtosis Kurtosis kurtosis0.594
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14140000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.420; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.479; Smooth: 0.814

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (3)

9. Files and Curves (10)