8ty0

Streptavidin variant S112E-K121H bound to bis-biotinylated Iron-porphyrin

Method: X-RAY DIFFRACTION Dmax: 67.1 Å Quality: REASONABLE

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

Streptavidin

Streptomyces avidinii

UniProt P22629

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 38–183 Chain B; UniProt 38–183 Chain C; UniProt 38–183 Chain D; UniProt 38–183 Not recorded SIK Bis-biotinylated Iron-porphyrin × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;293 K;0.2 M ammonium sulfate, 0.1 M sodium acetate pH 4.5 , 20% PEG 4000 Resolution 1.54 Å R-free 0.191

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.

312 other PDB entries and 368 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAV_STRAV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 13–158; UniProt 38–183 Author chain B; PDBConstruct 13–158; UniProt 38–183 Author chain C; PDBConstruct 13–158; UniProt 38–183 Author chain D; PDBConstruct 13–158; UniProt 38–183

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 8ty0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ty0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ty0
Deposition date deposition_date2023-08-24
Structure title titleStreptavidin variant S112E-K121H bound to bis-biotinylated Iron-porphyrin
Keywords keywordsArtificial metalloprotein, biotin-binding protein, streptavidin, artificial metalloenzyme, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.56
Radius of gyration Rg (electron density) rg_electron21.52
Forward intensity I(0) i055396700.00
Molecular weight molecular_weight55029.0 kDa
Excluded volume excluded_volume67352 ų
Envelope volume envelope_volume77017 ų
Hydration-shell volume shell_volume28397 ų
Envelope diameter envelope_diameter67.8
Shell Rg shell_rg29.39
Envelope Rg envelope_rg21.82
Shape Rg shape_rg21.49
Total Rg total_rg22.44
Total atoms total_atoms3997
Residues n_residues496
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 dmax67.1
Rg (real space) rg_real22.40
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real5.5400e+07
I(0) uncertainty (real space) i0_real_error6.1420e+05
Rg (reciprocal space) rg_reciprocal22.44
I(0) (reciprocal space) i0_reciprocal55400000.0000
Solution quality estimate total_estimate0.7305
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.5
Skewness Skewness skewness0.086
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27370000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 0.242; Positv: 1.000; Valcen: 0.977; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)