3rdx

Crystal structure of ligand-free R7-2 streptavidin

Method: X-RAY DIFFRACTION Dmax: 71.9 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 37–164 Chain B; UniProt 37–164 Fragment:UNP Residues 37-164 Mutation:T90S,W108V,L110T,F29L,S52G,R53S GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;0.1 M Na acetate, pH 4.5, 3 M sodium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.10 Å R-free 0.278
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 37–164 Chain B; UniProt 37–164 Fragment:UNP Residues 37-164 Mutation:T90S,W108V,L110T,F29L,S52G,R53S GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;0.1 M Na acetate, pH 4.5, 3 M sodium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.10 Å R-free 0.278

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 367 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 26–153; UniProt 37–164 Author chain B; PDBConstruct 26–153; UniProt 37–164

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 3rdx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3rdx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3rdx
Deposition date deposition_date2011-04-02
Structure title titleCrystal structure of ligand-free R7-2 streptavidin
Keywords keywordsStreptavidin variants, improved desthiobiotin binding, opened loop destabilization, BIOTIN BINDING PROTEIN; BIOTIN BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.30
Radius of gyration Rg (electron density) rg_electron21.54
Forward intensity I(0) i012789000.00
Molecular weight molecular_weight25839.0 kDa
Excluded volume excluded_volume31791 ų
Envelope volume envelope_volume40409 ų
Hydration-shell volume shell_volume16080 ų
Envelope diameter envelope_diameter66.2
Shell Rg shell_rg26.82
Envelope Rg envelope_rg21.46
Shape Rg shape_rg21.50
Total Rg total_rg22.36
Total atoms total_atoms1825
Residues n_residues249
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 dmax71.9
Rg (real space) rg_real22.28
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.2790e+07
I(0) uncertainty (real space) i0_real_error1.8050e+05
Rg (reciprocal space) rg_reciprocal22.29
I(0) (reciprocal space) i0_reciprocal12790000.0000
Solution quality estimate total_estimate0.8106
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.6
Skewness Skewness skewness0.162
Kurtosis Kurtosis kurtosis-0.826
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3220000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.948; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3rdxa1
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_idd3rdxa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3rdxb1
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_idd3rdxb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3rdxA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id3rdxB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like

8. Citations (1)

9. Files and Curves (10)