9csv

Streptavidin-E101Q-S112Y-K121A bound to Cu(II)-biotin-ethyl-dipicolylamine cofactor, oxidized by hydrogen peroxide

Method: X-RAY DIFFRACTION Dmax: 54.6 Å Quality: GOOD

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 Mutation:E101Q, S112Y, K121A QG7 N-(2-{bis[(pyridin-2-yl)methyl]amino}ethyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide × 4 CU COPPER (II) ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;ammonium sulfate, sodium acetate Resolution 1.60 Å R-free 0.234

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 14–159; 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 9csv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9csv
Deposition date deposition_date2024-07-24
Structure title titleStreptavidin-E101Q-S112Y-K121A bound to Cu(II)-biotin-ethyl-dipicolylamine cofactor, oxidized by hydrogen peroxide
Keywords keywordsbiotin-streptavidin complex, artificial metalloprotein, 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_guinier16.07
Radius of gyration Rg (electron density) rg_electron14.97
Forward intensity I(0) i03929800.00
Molecular weight molecular_weight13590.0 kDa
Excluded volume excluded_volume16720 ų
Envelope volume envelope_volume19144 ų
Hydration-shell volume shell_volume11402 ų
Envelope diameter envelope_diameter54.0
Shell Rg shell_rg19.92
Envelope Rg envelope_rg15.54
Shape Rg shape_rg14.93
Total Rg total_rg16.00
Total atoms total_atoms992
Residues n_residues123
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 dmax54.6
Rg (real space) rg_real16.09
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real3.9300e+06
I(0) uncertainty (real space) i0_real_error4.9120e+04
Rg (reciprocal space) rg_reciprocal16.09
I(0) (reciprocal space) i0_reciprocal3930000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.0
Skewness Skewness skewness0.384
Kurtosis Kurtosis kurtosis-0.252
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha622800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.812; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.945; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)