7b74

Chimeric Streptavidin With A Dimerization Domain For Artificial Transfer Hydrogenation

Method: X-RAY DIFFRACTION Dmax: 67.4 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Streptavidin,Superoxide dismutase [Cu-Zn],Streptavidin

Streptomyces avidinii

UniProt P0A609

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain AAA; UniProt 196–230 Chain BBB; UniProt 196–230 Chain CCC; UniProt 196–230 Chain DDD; UniProt 196–230 Not recorded 4IR {N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide}(chloro)[(1,2,3,4,5-eta)-1,2,3,4,5-pentamethylcyclopentadienyl]iridium(III) × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20 %w/v PEG 3350 (Polymer) 0.2 M KF (Salt) Resolution 1.85 Å R-free 0.218

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SODC_MYCBO
Isoform
PDB entities 1
Chains and sequence ranges Author chain AAA; PDBConstruct 49–83; UniProt 196–230 Author chain BBB; PDBConstruct 49–83; UniProt 196–230 Author chain CCC; PDBConstruct 49–83; UniProt 196–230 Author chain DDD; PDBConstruct 49–83; UniProt 196–230

Streptavidin,Superoxide dismutase [Cu-Zn],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 Insufficient information Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain AAA; UniProt 39–72 Chain AAA; UniProt 73–183 Chain BBB; UniProt 39–72 Chain BBB; UniProt 73–183 Chain CCC; UniProt 39–72 Chain CCC; UniProt 73–183 Chain DDD; UniProt 39–72 Chain DDD; UniProt 73–183 Not recorded 4IR {N-(4-{[2-(amino-kappaN)ethyl]sulfamoyl-kappaN}phenyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide}(chloro)[(1,2,3,4,5-eta)-1,2,3,4,5-pentamethylcyclopentadienyl]iridium(III) × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20 %w/v PEG 3350 (Polymer) 0.2 M KF (Salt) Resolution 1.85 Å R-free 0.218

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 AAA; PDBConstruct 15–48; UniProt 39–72 Author chain AAA; PDBConstruct 84–194; UniProt 73–183 Author chain BBB; PDBConstruct 15–48; UniProt 39–72 Author chain BBB; PDBConstruct 84–194; UniProt 73–183 Author chain CCC; PDBConstruct 15–48; UniProt 39–72 Author chain CCC; PDBConstruct 84–194; UniProt 73–183 Author chain DDD; PDBConstruct 15–48; UniProt 39–72 Author chain DDD; PDBConstruct 84–194; UniProt 73–183

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 7b74

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7b74
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7b74
Deposition date deposition_date2020-12-09
Structure title titleChimeric Streptavidin With A Dimerization Domain For Artificial Transfer Hydrogenation
Keywords keywordsArtificial tranfer hydrogenation biotin-binding protein artificial metalloenzyme, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.48
Radius of gyration Rg (electron density) rg_electron21.46
Forward intensity I(0) i054302700.00
Molecular weight molecular_weight54683.0 kDa
Excluded volume excluded_volume66901 ų
Envelope volume envelope_volume76637 ų
Hydration-shell volume shell_volume28258 ų
Envelope diameter envelope_diameter69.8
Shell Rg shell_rg29.44
Envelope Rg envelope_rg21.87
Shape Rg shape_rg21.48
Total Rg total_rg22.27
Total atoms total_atoms7252
Residues n_residues492
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 dmax67.4
Rg (real space) rg_real22.32
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real5.4300e+07
I(0) uncertainty (real space) i0_real_error6.9450e+05
Rg (reciprocal space) rg_reciprocal22.36
I(0) (reciprocal space) i0_reciprocal54300000.0000
Solution quality estimate total_estimate0.8266
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.108
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha20690000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.924; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)