1swb

APO-CORE-STREPTAVIDIN AT PH 7.5

Method: X-RAY DIFFRACTION Dmax: 69.0 Å Quality: REASONABLE

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 Fragment:CORE, RESIDUES 13 - 139 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;PROTEIN WAS CRYSTALLIZED FROM 48% MPD (2-METHYL-PENTANE-2,4-DIOLE, PH 4.5), 5.5H SOAKING IN 0.1M HEPES BUFFER PH 7.5 Resolution 1.85 Å R-free 0.253

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 1swb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1swb
Deposition date deposition_date1997-03-04
Structure title titleAPO-CORE-STREPTAVIDIN AT PH 7.5
Keywords keywordsBIOTIN BINDING PROTEIN, BIOTIN, 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_guinier23.01
Radius of gyration Rg (electron density) rg_electron21.92
Forward intensity I(0) i043758400.00
Molecular weight molecular_weight49307.0 kDa
Excluded volume excluded_volume60785 ų
Envelope volume envelope_volume73262 ų
Hydration-shell volume shell_volume27067 ų
Envelope diameter envelope_diameter70.7
Shell Rg shell_rg29.20
Envelope Rg envelope_rg22.00
Shape Rg shape_rg21.88
Total Rg total_rg22.86
Total atoms total_atoms3496
Residues n_residues465
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 dmax69.0
Rg (real space) rg_real22.85
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real4.3760e+07
I(0) uncertainty (real space) i0_real_error5.0010e+05
Rg (reciprocal space) rg_reciprocal22.89
I(0) (reciprocal space) i0_reciprocal43760000.0000
Solution quality estimate total_estimate0.6412
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.0
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.545
Angular range angular_range— – 0.3450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9476000.0000
Real-space data points n_real_points66
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 0.171; Positv: 1.000; Valcen: 0.981; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1swba_
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_idd1swbb_
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_idd1swbc_
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_idd1swbd_
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_id1swbA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1swbB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1swbC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1swbD00
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)