9v85

Superfolder GFP fused gp38 receptor binding domain of bacteriophage PP01

Method: X-RAY DIFFRACTION Dmax: 123.9 Å Quality: REASONABLE

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

Green fluorescent protein,Receptor-recognizing protein gp38

Escherichia phage PP01

UniProt A0A059PIQ0

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 3–238 Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;10% (w/v) PEG8000, 0.1M Na-HEPES-MOPS, pH7.5, 3mM CaCl2, 3mM MgCl2, 20 % (v/v) ethylene glycol Resolution 2.10 Å R-free 0.208
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 3–238 Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;10% (w/v) PEG8000, 0.1M Na-HEPES-MOPS, pH7.5, 3mM CaCl2, 3mM MgCl2, 20 % (v/v) ethylene glycol Resolution 2.10 Å R-free 0.208

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.

91 other PDB entries and 136 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A059PIQ0_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–235; UniProt 3–238 Author chain C; PDBConstruct 2–235; UniProt 3–238

Green fluorescent protein,Receptor-recognizing protein gp38

Escherichia phage PP01

UniProt A0A2Z5WK79

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 41–259 Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;10% (w/v) PEG8000, 0.1M Na-HEPES-MOPS, pH7.5, 3mM CaCl2, 3mM MgCl2, 20 % (v/v) ethylene glycol Resolution 2.10 Å R-free 0.208
2 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 41–259 Non-standard monomer:Yes (specific site not provided by mmCIF) CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;10% (w/v) PEG8000, 0.1M Na-HEPES-MOPS, pH7.5, 3mM CaCl2, 3mM MgCl2, 20 % (v/v) ethylene glycol Resolution 2.10 Å R-free 0.208

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 A0A2Z5WK79_9CAUD
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 240–458; UniProt 41–259 Author chain C; PDBConstruct 240–458; UniProt 41–259

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 9v85

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9v85
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9v85
Deposition date deposition_date2025-05-29
Structure title titleSuperfolder GFP fused gp38 receptor binding domain of bacteriophage PP01
Keywords keywordsphage host recognition, phage tail fiber, receptor binding protein, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.82
Radius of gyration Rg (electron density) rg_electron37.61
Forward intensity I(0) i081621600.00
Molecular weight molecular_weight69462.0 kDa
Excluded volume excluded_volume85402 ų
Envelope volume envelope_volume112180 ų
Hydration-shell volume shell_volume28050 ų
Envelope diameter envelope_diameter127.7
Shell Rg shell_rg38.77
Envelope Rg envelope_rg37.00
Shape Rg shape_rg37.58
Total Rg total_rg37.77
Total atoms total_atoms4905
Residues n_residues666
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 dmax123.9
Rg (real space) rg_real37.38
Rg uncertainty (real space) rg_real_error1.26
I(0) (real space) i0_real8.1620e+07
I(0) uncertainty (real space) i0_real_error1.3980e+06
Rg (reciprocal space) rg_reciprocal37.04
I(0) (reciprocal space) i0_reciprocal81590000.0000
Solution quality estimate total_estimate0.7182
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.9
Skewness Skewness skewness0.483
Kurtosis Kurtosis kurtosis-0.765
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5615000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.505; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.239; Smooth: 0.578

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)