5n8e

CRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE RDPAPAWAHGGG

Method: X-RAY DIFFRACTION Dmax: 66.1 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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–183 Chain B; UniProt 1–183 Chain C; UniProt 1–183 Chain D; UniProt 1–183 Not recorded ARG-ASP-PRO-ALA-PRO-ALA-TRP-ALA-HIS-GLY-GLY-GLY-NH2 × 3 NA SODIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4;293 K;0.2M Ammonium acetate 0.1M Sodium acetate pH 4 15% PEG4000 Resolution 1.10 Å R-free 0.153

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 1–183; UniProt 1–183 Author chain B; PDBConstruct 1–183; UniProt 1–183 Author chain C; PDBConstruct 1–183; UniProt 1–183 Author chain D; PDBConstruct 1–183; UniProt 1–183

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 5n8e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5n8e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5n8e
Deposition date deposition_date2017-02-23
Structure title titleCRYSTAL STRUCTURE OF STREPTAVIDIN WITH PEPTIDE RDPAPAWAHGGG
Keywords keywordsSTREPTAVIDIN, BIOTIN BINDING PROTEIN, STREPTAVIDIN PEPTIDE 11101 COMPLEX; BIOTIN BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.81
Radius of gyration Rg (electron density) rg_electron21.78
Forward intensity I(0) i051950100.00
Molecular weight molecular_weight54102.0 kDa
Excluded volume excluded_volume66694 ų
Envelope volume envelope_volume77882 ų
Hydration-shell volume shell_volume28491 ų
Envelope diameter envelope_diameter68.5
Shell Rg shell_rg29.46
Envelope Rg envelope_rg22.01
Shape Rg shape_rg21.74
Total Rg total_rg22.74
Total atoms total_atoms3836
Residues n_residues516
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 dmax66.1
Rg (real space) rg_real22.64
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real5.1950e+07
I(0) uncertainty (real space) i0_real_error6.6930e+05
Rg (reciprocal space) rg_reciprocal22.68
I(0) (reciprocal space) i0_reciprocal51950000.0000
Solution quality estimate total_estimate0.8354
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.1
Skewness Skewness skewness0.080
Kurtosis Kurtosis kurtosis-0.539
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15640000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.960; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.980; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id5n8eA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5n8eB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5n8eC00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id5n8eD00
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)