3rdm

Crystal structure of R7-2 streptavidin complexed with biotin/PEG

Method: X-RAY DIFFRACTION Dmax: 53.7 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 37–164 Fragment:UNP Residues 37-164 Mutation:T90S, W108V, L110T, F29L, S52G, R53S 1PE PENTAETHYLENE GLYCOL × 1 BTN BIOTIN × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;298 K;0.2 MgCl2, 0.1 Bis-Tris, pH 5.5, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.60 Å R-free 0.245
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 37–164 Fragment:UNP Residues 37-164 Mutation:T90S, W108V, L110T, F29L, S52G, R53S 1PE PENTAETHYLENE GLYCOL × 4 BTN BIOTIN × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;298 K;0.2 MgCl2, 0.1 Bis-Tris, pH 5.5, 25% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 1.60 Å R-free 0.245

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 A; PDBConstruct 26–153; UniProt 37–164

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 3rdm

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3rdm
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3rdm
Deposition date deposition_date2011-04-01
Structure title titleCrystal structure of R7-2 streptavidin complexed with biotin/PEG
Keywords keywordsStreptavidin variants, improved desthiobiotin binding, opened loop destabilization, 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_guinier16.03
Radius of gyration Rg (electron density) rg_electron14.91
Forward intensity I(0) i03626400.00
Molecular weight molecular_weight12932.0 kDa
Excluded volume excluded_volume15943 ų
Envelope volume envelope_volume18853 ų
Hydration-shell volume shell_volume11270 ų
Envelope diameter envelope_diameter53.6
Shell Rg shell_rg19.90
Envelope Rg envelope_rg15.55
Shape Rg shape_rg14.89
Total Rg total_rg15.98
Total atoms total_atoms914
Residues n_residues123
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 dmax53.7
Rg (real space) rg_real16.04
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real3.6260e+06
I(0) uncertainty (real space) i0_real_error3.6590e+04
Rg (reciprocal space) rg_reciprocal16.04
I(0) (reciprocal space) i0_reciprocal3626000.0000
Solution quality estimate total_estimate0.8789
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.0
Skewness Skewness skewness0.383
Kurtosis Kurtosis kurtosis-0.235
Angular range angular_range— – 0.4950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha530200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.832; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; Smooth: 0.964

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3rdma1
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_idd3rdma2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id3rdmA00
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)