1n43

Streptavidin Mutant N23A with biotin at 1.89A

Method: X-RAY DIFFRACTION Dmax: 66.0 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 Fragment:core streptavidin, residues 13-139 Mutation:N23A BTN BIOTIN × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.5;293 K;MPD, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.89 Å R-free 0.301

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 1n43

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1n43
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1n43
Deposition date deposition_date2002-10-30
Structure title titleStreptavidin Mutant N23A with biotin at 1.89A
Keywords keywordstetramer, 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_guinier22.18
Radius of gyration Rg (electron density) rg_electron21.09
Forward intensity I(0) i045123500.00
Molecular weight molecular_weight50468.0 kDa
Excluded volume excluded_volume62261 ų
Envelope volume envelope_volume70233 ų
Hydration-shell volume shell_volume26590 ų
Envelope diameter envelope_diameter67.5
Shell Rg shell_rg28.58
Envelope Rg envelope_rg21.38
Shape Rg shape_rg21.07
Total Rg total_rg21.98
Total atoms total_atoms3573
Residues n_residues471
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 dmax66.0
Rg (real space) rg_real21.99
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real4.5120e+07
I(0) uncertainty (real space) i0_real_error5.1420e+05
Rg (reciprocal space) rg_reciprocal22.02
I(0) (reciprocal space) i0_reciprocal45120000.0000
Solution quality estimate total_estimate0.8324
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.090
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.3600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13290000.0000
Real-space data points n_real_points68
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1n43a_
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_idd1n43b_
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_idd1n43c_
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_idd1n43d_
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_id1n43A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1n43B00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1n43C00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id1n43D00
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)