1moy

Streptavidin Mutant with Osteopontin Hexapeptide Insertion Including RGD

Method: X-RAY DIFFRACTION Dmax: 62.6 Å Quality: REASONABLE

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 Fragment:core streptavidin, residues 13-139 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 8 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 1.55 Å R-free 0.185
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 37–163 Fragment:core streptavidin, residues 13-139 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 8 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 1.55 Å R-free 0.185
3 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 37–163 Fragment:core streptavidin, residues 13-139 MRD (4R)-2-METHYLPENTANE-2,4-DIOL × 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 1.55 Å R-free 0.185

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 366 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 1–130; 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 1moy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1moy
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1moy
Deposition date deposition_date2002-09-10
Structure title titleStreptavidin Mutant with Osteopontin Hexapeptide Insertion Including RGD
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_guinier16.65
Radius of gyration Rg (electron density) rg_electron15.36
Forward intensity I(0) i03808050.00
Molecular weight molecular_weight13336.0 kDa
Excluded volume excluded_volume16495 ų
Envelope volume envelope_volume20002 ų
Hydration-shell volume shell_volume11600 ų
Envelope diameter envelope_diameter57.1
Shell Rg shell_rg20.38
Envelope Rg envelope_rg16.26
Shape Rg shape_rg15.33
Total Rg total_rg16.47
Total atoms total_atoms944
Residues n_residues124
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 dmax62.6
Rg (real space) rg_real16.67
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real3.8080e+06
I(0) uncertainty (real space) i0_real_error5.5610e+04
Rg (reciprocal space) rg_reciprocal16.67
I(0) (reciprocal space) i0_reciprocal3808000.0000
Solution quality estimate total_estimate0.7385
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks4
Primary peak position r_peak_primary18.7
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.223
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha479700.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.593; Stabil: 0.986; Sysdev: 1.000; Positv: 1.000; Valcen: 0.860; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1moya_
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 (1 domains)

Domain ID domain_id1moyA00
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)