6s4q

scdSav(SASK) - Engineering Single-Chain Dimeric Streptavidin as Host for Artificial Metalloenzymes

Method: X-RAY DIFFRACTION Dmax: 65.2 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 39–183 Chain A; UniProt 39–183 Chain B; UniProt 39–183 Chain B; UniProt 39–183 Not recorded 4IR {N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide}(chloro)[(1,2,3,4,5-eta)-1,2,3,4,5-pentamethylcyclopentadienyl]iridium(III) × 4 GOL GLYCEROL × 5 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 1.85 Å R-free 0.231

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 15–159; UniProt 39–183 Author chain A; PDBConstruct 199–343; UniProt 39–183 Author chain B; PDBConstruct 15–159; UniProt 39–183 Author chain B; PDBConstruct 199–343; 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 6s4q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6s4q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6s4q
Deposition date deposition_date2019-06-28
Structure title titlescdSav(SASK) - Engineering Single-Chain Dimeric Streptavidin as Host for Artificial Metalloenzymes
Keywords keywordsBiotin-Binding Protein, Artificial Transfer Hydrogenase, Beta Barrel, Streptavidin, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.25
Radius of gyration Rg (electron density) rg_electron21.31
Forward intensity I(0) i055564800.00
Molecular weight molecular_weight54993.0 kDa
Excluded volume excluded_volume67093 ų
Envelope volume envelope_volume75811 ų
Hydration-shell volume shell_volume28122 ų
Envelope diameter envelope_diameter67.2
Shell Rg shell_rg29.27
Envelope Rg envelope_rg21.73
Shape Rg shape_rg21.34
Total Rg total_rg22.07
Total atoms total_atoms3827
Residues n_residues487
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 dmax65.2
Rg (real space) rg_real22.10
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real5.5560e+07
I(0) uncertainty (real space) i0_real_error6.6730e+05
Rg (reciprocal space) rg_reciprocal22.14
I(0) (reciprocal space) i0_reciprocal55570000.0000
Solution quality estimate total_estimate0.8315
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.6
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.483
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23910000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.943; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd6s4qa1
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6s4qa2
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6s4qa3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6s4qb1
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6s4qb2
Class classb — All beta proteins
Fold Fold foldb.61 — Streptavidin-like
Superfamily Superfamily superfamilyb.61.1 — Avidin/streptavidin
Family Family familyb.61.1.1 — Avidin/streptavidin
Domain ID domain_idd6s4qb3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)