3ry1

Wild-type core streptavidin at atomic resolution

Method: X-RAY DIFFRACTION Dmax: 74.3 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 37–163 Chain B; UniProt 37–163 Chain C; UniProt 37–163 Chain D; UniProt 37–163 Not recorded MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 3 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 7 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;298 K;52% MPD, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.03 Å R-free 0.135

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 1–127; UniProt 37–163 Author chain B; PDBConstruct 1–127; UniProt 37–163 Author chain C; PDBConstruct 1–127; UniProt 37–163 Author chain D; PDBConstruct 1–127; UniProt 37–163

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 3ry1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ry1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ry1
Deposition date deposition_date2011-05-10
Structure title titleWild-type core streptavidin at atomic resolution
Keywords keywordsbiotin-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_guinier23.02
Radius of gyration Rg (electron density) rg_electron21.85
Forward intensity I(0) i047003500.00
Molecular weight molecular_weight52080.0 kDa
Excluded volume excluded_volume64641 ų
Envelope volume envelope_volume75765 ų
Hydration-shell volume shell_volume27746 ų
Envelope diameter envelope_diameter75.5
Shell Rg shell_rg29.45
Envelope Rg envelope_rg22.20
Shape Rg shape_rg21.82
Total Rg total_rg22.82
Total atoms total_atoms3689
Residues n_residues490
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 dmax74.3
Rg (real space) rg_real22.86
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real4.7000e+07
I(0) uncertainty (real space) i0_real_error6.0350e+05
Rg (reciprocal space) rg_reciprocal22.90
I(0) (reciprocal space) i0_reciprocal47000000.0000
Solution quality estimate total_estimate0.8896
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.7
Skewness Skewness skewness0.100
Kurtosis Kurtosis kurtosis-0.515
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11080000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.858; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.996

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_idd3ry1a_
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_idd3ry1b_
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_idd3ry1c_
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_idd3ry1d_
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_id3ry1A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id3ry1B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id3ry1C00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id3ry1D00
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)