1swc

APO-CORE-STREPTAVIDIN AT PH 4.5

Method: X-RAY DIFFRACTION Dmax: 69.1 Å Quality: EXCELLENT

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 60% MPD (2-METHYL-PENTANE-2,4-DIOLE, PH 4.5), SOAKING IN 20 MM SODIUM ACETATE BUFFER PH 4.5 Resolution 1.80 Å R-free 0.232

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 1swc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1swc
Deposition date deposition_date1997-03-04
Structure title titleAPO-CORE-STREPTAVIDIN AT PH 4.5
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_guinier22.84
Radius of gyration Rg (electron density) rg_electron21.74
Forward intensity I(0) i043108000.00
Molecular weight molecular_weight48767.0 kDa
Excluded volume excluded_volume60046 ų
Envelope volume envelope_volume71102 ų
Hydration-shell volume shell_volume26546 ų
Envelope diameter envelope_diameter68.8
Shell Rg shell_rg28.90
Envelope Rg envelope_rg21.82
Shape Rg shape_rg21.71
Total Rg total_rg22.67
Total atoms total_atoms3458
Residues n_residues461
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 dmax69.1
Rg (real space) rg_real22.68
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real4.3110e+07
I(0) uncertainty (real space) i0_real_error5.8730e+05
Rg (reciprocal space) rg_reciprocal22.72
I(0) (reciprocal space) i0_reciprocal43110000.0000
Solution quality estimate total_estimate0.9069
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.0
Skewness Skewness skewness0.095
Kurtosis Kurtosis kurtosis-0.544
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8596000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.939; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.989

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_idd1swca_
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_idd1swcb_
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_idd1swcc_
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_idd1swcd_
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_id1swcA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1swcB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1swcC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1swcD00
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)