5to2

Crystal structure of streptavidin with one wild type subunit and three mutated subunits (N23A/S27D/S45A)

Method: X-RAY DIFFRACTION Dmax: 69.8 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 39–163 Chain B; UniProt 39–163 Chain C; UniProt 39–163 Chain D; UniProt 39–162 Mutation:N23A, S27D, S45A PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M Tris pH 8.3, 0.25 M MgCl2, 32% PEG4K Resolution 1.65 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, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–125; UniProt 39–163 Author chain B; PDBConstruct 1–125; UniProt 39–163 Author chain C; PDBConstruct 1–125; UniProt 39–163 Author chain D; PDBConstruct 1–124; UniProt 39–162

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 5to2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5to2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5to2
Deposition date deposition_date2016-10-16
Structure title titleCrystal structure of streptavidin with one wild type subunit and three mutated subunits (N23A/S27D/S45A)
Keywords keywordsStreptavidin, 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_guinier22.87
Radius of gyration Rg (electron density) rg_electron21.77
Forward intensity I(0) i045371900.00
Molecular weight molecular_weight50589.0 kDa
Excluded volume excluded_volume62538 ų
Envelope volume envelope_volume75123 ų
Hydration-shell volume shell_volume27693 ų
Envelope diameter envelope_diameter69.2
Shell Rg shell_rg29.31
Envelope Rg envelope_rg21.96
Shape Rg shape_rg21.73
Total Rg total_rg22.75
Total atoms total_atoms3587
Residues n_residues482
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 dmax69.8
Rg (real space) rg_real22.70
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real4.5370e+07
I(0) uncertainty (real space) i0_real_error5.6770e+05
Rg (reciprocal space) rg_reciprocal22.74
I(0) (reciprocal space) i0_reciprocal45370000.0000
Solution quality estimate total_estimate0.8281
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.084
Kurtosis Kurtosis kurtosis-0.540
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10530000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.927; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5to2a_
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_idd5to2b_
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_idd5to2c_
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_idd5to2d_
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

CATH v4.4 (4 domains)

Domain ID domain_id5to2A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5to2B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5to2C00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5to2D00
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)