6y3q

Streptavidin mutant S112R_K121E with a biotC5-1 cofactor - an artificial iron hydroxylase

Method: X-RAY DIFFRACTION Dmax: 53.8 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 AAA; UniProt 39–183 Not recorded O7Q biotC5-1 cofactor × 4 SO4 SULFATE ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;293 K;2 M (NH4)2SO4, 0.1 M Na-Acetate, pH 4 Resolution 1.95 Å R-free 0.258

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 AAA; PDBConstruct 15–159; UniProt 39–183

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 6y3q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6y3q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6y3q
Deposition date deposition_date2020-02-18
Structure title titleStreptavidin mutant S112R_K121E with a biotC5-1 cofactor - an artificial iron hydroxylase
Keywords keywordsArtificial Metalloenzyme, Iron Hydroxylase, Biotin-Binding Protein, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.02
Radius of gyration Rg (electron density) rg_electron14.79
Forward intensity I(0) i03782110.00
Molecular weight molecular_weight13061.0 kDa
Excluded volume excluded_volume15996 ų
Envelope volume envelope_volume18758 ų
Hydration-shell volume shell_volume11270 ų
Envelope diameter envelope_diameter53.5
Shell Rg shell_rg19.89
Envelope Rg envelope_rg15.43
Shape Rg shape_rg14.76
Total Rg total_rg15.88
Total atoms total_atoms1763
Residues n_residues120
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 dmax53.8
Rg (real space) rg_real16.03
Rg uncertainty (real space) rg_real_error0.25
I(0) (real space) i0_real3.7820e+06
I(0) uncertainty (real space) i0_real_error4.4010e+04
Rg (reciprocal space) rg_reciprocal16.03
I(0) (reciprocal space) i0_reciprocal3782000.0000
Solution quality estimate total_estimate0.7473
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.4
Skewness Skewness skewness0.371
Kurtosis Kurtosis kurtosis-0.243
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha512400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.831; Stabil: 1.000; Sysdev: 0.424; Positv: 1.000; Valcen: 0.964; Smooth: 0.982

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)