3osq

Maltose-bound maltose sensor engineered by insertion of circularly permuted green fluorescent protein into E. coli maltose binding protein at position 175

Method: X-RAY DIFFRACTION Dmax: 92.9 Å Quality: GOOD

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

Maltose-binding periplasmic protein,Green fluorescent protein

Escherichia coli O157:H7

UniProt P0AEY0

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 27–199 Chain A; UniProt 200–396 Fragment:GFP P42212 residues 2-146, 147-238, MBP P0AEX9 residues 27-199, 201-396 Non-standard monomer:Yes (specific site not provided by mmCIF) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;296 K;0.5 M Ammonium sulfate, 0.1M Sodium citrate tribasic dihydrate pH 5.6, 1.0 M Lithium sulfate monohydrate, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 1.90 Å R-free 0.199

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.

109 other PDB entries and 148 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECO57
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 37–209; UniProt 27–199 Author chain A; PDBConstruct 456–652; UniProt 200–396

Maltose-binding periplasmic protein,Green fluorescent protein

Escherichia coli O157:H7

UniProt P42212

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 147–238 Chain A; UniProt 2–146 Fragment:GFP P42212 residues 2-146, 147-238, MBP P0AEX9 residues 27-199, 201-396 Non-standard monomer:Yes (specific site not provided by mmCIF) alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 1 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;296 K;0.5 M Ammonium sulfate, 0.1M Sodium citrate tribasic dihydrate pH 5.6, 1.0 M Lithium sulfate monohydrate, VAPOR DIFFUSION, HANGING DROP, temperature 296K Resolution 1.90 Å R-free 0.199

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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 212–303; UniProt 147–238 Author chain A; PDBConstruct 312–454; UniProt 2–146

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 3osq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3osq
Deposition date deposition_date2010-09-09
Structure title titleMaltose-bound maltose sensor engineered by insertion of circularly permuted green fluorescent protein into E. coli maltose binding protein at position 175
Keywords keywordsEngineered Protein, Sensor Protein, Fluorescent Protein, MBP, GFP, Maltose Sensor, Transport Protein; FLUORESCENT PROTEIN, Transport Protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.06
Radius of gyration Rg (electron density) rg_electron28.33
Forward intensity I(0) i072532300.00
Molecular weight molecular_weight68208.0 kDa
Excluded volume excluded_volume85868 ų
Envelope volume envelope_volume104920 ų
Hydration-shell volume shell_volume31311 ų
Envelope diameter envelope_diameter99.0
Shell Rg shell_rg34.86
Envelope Rg envelope_rg28.46
Shape Rg shape_rg28.28
Total Rg total_rg29.12
Total atoms total_atoms4816
Residues n_residues607
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 dmax92.9
Rg (real space) rg_real29.08
Rg uncertainty (real space) rg_real_error0.58
I(0) (real space) i0_real7.2530e+07
I(0) uncertainty (real space) i0_real_error1.0130e+06
Rg (reciprocal space) rg_reciprocal29.07
I(0) (reciprocal space) i0_reciprocal72530000.0000
Solution quality estimate total_estimate0.8993
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.7
Skewness Skewness skewness0.322
Kurtosis Kurtosis kurtosis-0.546
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha23570000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.922; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id3osqA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3osqA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id3osqA03
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein

8. Citations (1)

9. Files and Curves (10)