2rtp

STREPTAVIDIN-2-IMINOBIOTIN COMPLEX, PH 3.25, SPACE GROUP I222

Method: X-RAY DIFFRACTION Dmax: 58.6 Å Quality: REASONABLE

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

STREPTAVIDIN

OrganismNot specified

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 B; UniProt 25–159 Chain D; UniProt 25–159 Not recorded IMI 2-IMINOBIOTIN × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 3.25;ROOM TEMPERATURE, PH 3.25. SYNTHETIC MOTHER LIQUOR OF 50% SATURATED AMMONIUM SULFATE, 50% 1 M POTASSIUM ACETATE, 170 MM 2-IMINOBIOTIN, PH ADJUSTED TO 3.25 Resolution 1.50 Å R-free 0.243
2 Protein homooligomer Homooligomer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 25–159 Chain D; UniProt 25–159 Not recorded IMI 2-IMINOBIOTIN × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 3.25;ROOM TEMPERATURE, PH 3.25. SYNTHETIC MOTHER LIQUOR OF 50% SATURATED AMMONIUM SULFATE, 50% 1 M POTASSIUM ACETATE, 170 MM 2-IMINOBIOTIN, PH ADJUSTED TO 3.25 Resolution 1.50 Å R-free 0.243

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 367 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 B; PDBConstruct 1–135; UniProt 25–159 Author chain D; PDBConstruct 1–135; UniProt 25–159

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 2rtp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2rtp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2rtp
Deposition date deposition_date1997-09-11
Structure title titleSTREPTAVIDIN-2-IMINOBIOTIN COMPLEX, PH 3.25, SPACE GROUP I222
Keywords keywordsBIOTIN-BINDING PROTEIN, STREPTAVIDIN-2-IMINOBIOTIN, PH 3.25; BIOTIN-BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.08
Radius of gyration Rg (electron density) rg_electron16.94
Forward intensity I(0) i013216600.00
Molecular weight molecular_weight26152.0 kDa
Excluded volume excluded_volume32220 ų
Envelope volume envelope_volume36429 ų
Hydration-shell volume shell_volume17651 ų
Envelope diameter envelope_diameter58.7
Shell Rg shell_rg23.44
Envelope Rg envelope_rg17.38
Shape Rg shape_rg16.92
Total Rg total_rg17.98
Total atoms total_atoms3589
Residues n_residues244
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 dmax58.6
Rg (real space) rg_real17.96
Rg uncertainty (real space) rg_real_error0.29
I(0) (real space) i0_real1.3220e+07
I(0) uncertainty (real space) i0_real_error1.5230e+05
Rg (reciprocal space) rg_reciprocal17.98
I(0) (reciprocal space) i0_reciprocal13220000.0000
Solution quality estimate total_estimate0.7211
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.174
Kurtosis Kurtosis kurtosis-0.430
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3292000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 0.275; Positv: 1.000; Valcen: 0.994; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2rtpb_
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_idd2rtpd_
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 (2 domains)

Domain ID domain_id2rtpB00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like
Domain ID domain_id2rtpD00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily30 — Avidin-like

8. Citations (8)

9. Files and Curves (10)