2y3f

Traptavidin, biotin bound form

Method: X-RAY DIFFRACTION Dmax: 56.5 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 Fragment:RESIDUES 37-163 Mutation:YES BTN BIOTIN × 4 GOL GLYCEROL × 12 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8.5;27% PEG 4000, 0.25M MGCL2, 0.1M TRIS-HCL PH 8.5 Resolution 1.49 Å R-free 0.151

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 2–128; 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 2y3f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2y3f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2y3f
Deposition date deposition_date2010-12-20
Structure title titleTraptavidin, biotin bound form
Keywords keywordsBIOTIN-BINDING PROTEIN, PROTEIN ENGINEERING; BIOTIN-BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.03
Radius of gyration Rg (electron density) rg_electron14.90
Forward intensity I(0) i03686940.00
Molecular weight molecular_weight13185.0 kDa
Excluded volume excluded_volume16277 ų
Envelope volume envelope_volume19184 ų
Hydration-shell volume shell_volume11407 ų
Envelope diameter envelope_diameter55.9
Shell Rg shell_rg20.10
Envelope Rg envelope_rg15.73
Shape Rg shape_rg14.85
Total Rg total_rg16.04
Total atoms total_atoms932
Residues n_residues121
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 dmax56.5
Rg (real space) rg_real16.06
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real3.6870e+06
I(0) uncertainty (real space) i0_real_error4.1620e+04
Rg (reciprocal space) rg_reciprocal16.06
I(0) (reciprocal space) i0_reciprocal3687000.0000
Solution quality estimate total_estimate0.8549
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.9
Skewness Skewness skewness0.421
Kurtosis Kurtosis kurtosis-0.132
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha582800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.736; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.908; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2y3fa_
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 (1 domains)

Domain ID domain_id2y3fA00
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)