6udc

Spectroscopic and structural characterization of a genetically encoded direct sensor for protein-ligand interactions

Method: X-RAY DIFFRACTION Dmax: 67.9 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 Non-standard monomer:Yes (specific site not provided by mmCIF) BTN BIOTIN × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;500 ul of 0.1 M Bis-Tris, pH 6.5, 25% w/v polyethylene glycol 3350 in the reservoir with 2 ul of reservoir buffer mixed with 2 ul of 10 mg/ml of protein in the drop Resolution 2.10 Å R-free 0.256

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 2–128; UniProt 37–163 Author chain B; PDBConstruct 2–128; UniProt 37–163 Author chain C; PDBConstruct 2–128; UniProt 37–163 Author chain D; PDBConstruct 2–128; 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 6udc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6udc
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6udc
Deposition date deposition_date2019-09-19
Structure title titleSpectroscopic and structural characterization of a genetically encoded direct sensor for protein-ligand interactions
Keywords keywords;unnatural amino acid, non-canonical amino acid, fluorescence, biosensor, small molecule biosensor, ligand detection, FLUORESCENT PROTEIN ;; FLUORESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.44
Radius of gyration Rg (electron density) rg_electron21.37
Forward intensity I(0) i048690000.00
Molecular weight molecular_weight52184.0 kDa
Excluded volume excluded_volume64255 ų
Envelope volume envelope_volume74289 ų
Hydration-shell volume shell_volume27622 ų
Envelope diameter envelope_diameter66.8
Shell Rg shell_rg29.13
Envelope Rg envelope_rg21.73
Shape Rg shape_rg21.33
Total Rg total_rg22.33
Total atoms total_atoms3696
Residues n_residues477
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 dmax67.9
Rg (real space) rg_real22.28
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real4.8690e+07
I(0) uncertainty (real space) i0_real_error5.7990e+05
Rg (reciprocal space) rg_reciprocal22.32
I(0) (reciprocal space) i0_reciprocal48690000.0000
Solution quality estimate total_estimate0.9030
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.8
Skewness Skewness skewness0.091
Kurtosis Kurtosis kurtosis-0.534
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18830000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6udca_
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_idd6udcb_
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_idd6udcc_
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_idd6udcd_
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

8. Citations (1)

9. Files and Curves (10)