4osd

Dimer of a C-terminal fragment of phage T4 gp5 beta-helix

Method: X-RAY DIFFRACTION Dmax: 155.0 Å Quality: GOOD

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

Tail-associated lysozyme

Enterobacteria phage T4

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 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 484–575 Chain B; UniProt 484–575 Chain C; UniProt 484–575 Chain D; UniProt 484–575 Chain E; UniProt 484–575 Chain F; UniProt 484–575 Fragment:C-terminal fragment, UNP RESIDUES 484-575 ELA Elaidic acid × 3 MG MAGNESIUM ION × 2 STE STEARIC ACID × 2 PLM PALMITIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;22% PEG 4000, 200mM Li2SO4, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.96 Å R-free 0.279
2 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 484–575 Chain H; UniProt 484–575 Chain I; UniProt 484–575 Chain J; UniProt 484–575 Chain K; UniProt 484–575 Chain L; UniProt 484–575 Fragment:C-terminal fragment, UNP RESIDUES 484-575 ELA Elaidic acid × 2 MG MAGNESIUM ION × 2 STE STEARIC ACID × 2 PLM PALMITIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;22% PEG 4000, 200mM Li2SO4, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.96 Å R-free 0.279
3 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain M; UniProt 484–575 Chain N; UniProt 484–575 Chain O; UniProt 484–575 Chain P; UniProt 484–575 Chain Q; UniProt 484–575 Chain R; UniProt 484–575 Fragment:C-terminal fragment, UNP RESIDUES 484-575 ELA Elaidic acid × 2 MG MAGNESIUM ION × 2 STE STEARIC ACID × 2 PLM PALMITIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;291 K;22% PEG 4000, 200mM Li2SO4, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.96 Å R-free 0.279

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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name VG05_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–95; UniProt 484–575 Author chain B; PDBConstruct 4–95; UniProt 484–575 Author chain C; PDBConstruct 4–95; UniProt 484–575 Author chain D; PDBConstruct 4–95; UniProt 484–575 Author chain E; PDBConstruct 4–95; UniProt 484–575 Author chain F; PDBConstruct 4–95; UniProt 484–575 Author chain G; PDBConstruct 4–95; UniProt 484–575 Author chain H; PDBConstruct 4–95; UniProt 484–575 Author chain I; PDBConstruct 4–95; UniProt 484–575 Author chain J; PDBConstruct 4–95; UniProt 484–575 Author chain K; PDBConstruct 4–95; UniProt 484–575 Author chain L; PDBConstruct 4–95; UniProt 484–575 Author chain M; PDBConstruct 4–95; UniProt 484–575 Author chain N; PDBConstruct 4–95; UniProt 484–575 Author chain O; PDBConstruct 4–95; UniProt 484–575 Author chain P; PDBConstruct 4–95; UniProt 484–575 Author chain Q; PDBConstruct 4–95; UniProt 484–575 Author chain R; PDBConstruct 4–95; UniProt 484–575

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 4osd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4osd
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4osd
Deposition date deposition_date2014-02-12
Structure title titleDimer of a C-terminal fragment of phage T4 gp5 beta-helix
Keywords keywords;membrane piercing, T4 gp5, triple beta-helix, SDS resistant, donor strand exchange, fragment, membrane piercing complex, gp5.4, gp27-gp5 complex, HYDROLASE ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.62
Radius of gyration Rg (electron density) rg_electron44.43
Forward intensity I(0) i0499759000.00
Molecular weight molecular_weight178470.0 kDa
Excluded volume excluded_volume221400 ų
Envelope volume envelope_volume288050 ų
Hydration-shell volume shell_volume56501 ų
Envelope diameter envelope_diameter169.6
Shell Rg shell_rg46.05
Envelope Rg envelope_rg44.35
Shape Rg shape_rg44.38
Total Rg total_rg44.65
Total atoms total_atoms12510
Residues n_residues1672
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 dmax155.0
Rg (real space) rg_real43.90
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real4.9980e+08
I(0) uncertainty (real space) i0_real_error9.1640e+06
Rg (reciprocal space) rg_reciprocal43.62
I(0) (reciprocal space) i0_reciprocal499600000.0000
Solution quality estimate total_estimate0.8348
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.7
Skewness Skewness skewness0.584
Kurtosis Kurtosis kurtosis0.102
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37610000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.714; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.937; Smooth: 0.767

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)