9mfz

Streptavidin-E101Q-K121A-L124E bound to Fe(III)-biotin-pentyl-dipicolylamine cofactor

Method: X-RAY DIFFRACTION Dmax: 68.5 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 38–158 Chain B; UniProt 38–158 Chain C; UniProt 38–158 Chain D; UniProt 38–158 Mutation:E101Q, K121A, L124E A1BLH N-(5-{bis[(pyridin-2-yl)methyl]amino}pentyl)-5-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]pentanamide × 4 FE FE (III) ION × 8 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;298 K;ammonium sulfate, sodium acetate Resolution 1.55 Å R-free 0.189

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 5–125; UniProt 38–158 Author chain B; PDBConstruct 5–125; UniProt 38–158 Author chain C; PDBConstruct 5–125; UniProt 38–158 Author chain D; PDBConstruct 5–125; UniProt 38–158

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 9mfz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mfz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mfz
Deposition date deposition_date2024-12-10
最后修订 last_revision2025-12-17
Structure title titleStreptavidin-E101Q-K121A-L124E bound to Fe(III)-biotin-pentyl-dipicolylamine cofactor
Keywords keywordsbiotin-streptavidin complex, artificial metalloprotein, 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_guinier22.66
Radius of gyration Rg (electron density) rg_electron21.63
Forward intensity I(0) i099162100.00
Molecular weight molecular_weight51927.0 kDa
Excluded volume excluded_volume50076 ų
Envelope volume envelope_volume77860 ų
Hydration-shell volume shell_volume28509 ų
Envelope diameter envelope_diameter69.3
Shell Rg shell_rg29.55
Envelope Rg envelope_rg22.01
Shape Rg shape_rg21.44
Total Rg total_rg22.56
Total atoms total_atoms4046
Residues n_residues500
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 dmax68.5
Rg (real space) rg_real22.50
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real9.9160e+07
I(0) uncertainty (real space) i0_real_error1.1220e+06
Rg (reciprocal space) rg_reciprocal22.54
I(0) (reciprocal space) i0_reciprocal99160000.0000
Solution quality estimate total_estimate0.9044
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.5
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.531
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37520000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)