1stp

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Method: X-RAY DIFFRACTION Dmax: 55.0 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

STREPTAVIDIN COMPLEX WITH BIOTIN

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 25–183 Not recorded BTN BIOTIN × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.60 Å

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 1–159; UniProt 25–183

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 1stp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1stp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1stp
Deposition date deposition_date1992-03-12
Structure title titleSTRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN
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_guinier15.95
Radius of gyration Rg (electron density) rg_electron14.85
Forward intensity I(0) i03621720.00
Molecular weight molecular_weight12955.0 kDa
Excluded volume excluded_volume15950 ų
Envelope volume envelope_volume18584 ų
Hydration-shell volume shell_volume11193 ų
Envelope diameter envelope_diameter55.1
Shell Rg shell_rg19.71
Envelope Rg envelope_rg15.53
Shape Rg shape_rg14.82
Total Rg total_rg15.89
Total atoms total_atoms917
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 dmax55.0
Rg (real space) rg_real15.97
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real3.6220e+06
I(0) uncertainty (real space) i0_real_error4.1640e+04
Rg (reciprocal space) rg_reciprocal15.97
I(0) (reciprocal space) i0_reciprocal3622000.0000
Solution quality estimate total_estimate0.8663
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.405
Kurtosis Kurtosis kurtosis-0.160
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha534500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.943; Smooth: 0.991

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1stpa_
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_id1stpA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like

8. Citations (2)

9. Files and Curves (10)