9ebx

Chimeric fluorescence biosensor formed from a lactate-binding protein and GFP

Method: X-RAY DIFFRACTION Dmax: 104.9 Å Quality: GOOD

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

Green fluorescent protein,Methyl-accepting chemotaxis transducer (TlpC)

Aequorea victoria

UniProt O24911

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 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 30–292 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;296 K;magnesium chloride hexahydrate, HEPES, PEG 3350 Resolution 2.42 Å R-free 0.280

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.

2 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O24911_HELPY
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 159–421; UniProt 30–292

Green fluorescent protein,Methyl-accepting chemotaxis transducer (TlpC)

Aequorea victoria

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 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–146 Chain A; UniProt 149–238 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;296 K;magnesium chloride hexahydrate, HEPES, PEG 3350 Resolution 2.42 Å R-free 0.280

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 11–153; UniProt 2–146 Author chain A; PDBConstruct 426–515; UniProt 149–238

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 9ebx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9ebx
Deposition date deposition_date2024-11-13
Structure title titleChimeric fluorescence biosensor formed from a lactate-binding protein and GFP
Keywords keywordsBiosensor, Binding protein, Chimera, FLUORESCENT PROTEIN; FLUORESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.31
Radius of gyration Rg (electron density) rg_electron31.27
Forward intensity I(0) i040796500.00
Molecular weight molecular_weight49706.0 kDa
Excluded volume excluded_volume61889 ų
Envelope volume envelope_volume81614 ų
Hydration-shell volume shell_volume23736 ų
Envelope diameter envelope_diameter109.4
Shell Rg shell_rg35.15
Envelope Rg envelope_rg31.07
Shape Rg shape_rg31.23
Total Rg total_rg31.79
Total atoms total_atoms3517
Residues n_residues480
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 dmax104.9
Rg (real space) rg_real31.74
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real4.0800e+07
I(0) uncertainty (real space) i0_real_error6.5790e+05
Rg (reciprocal space) rg_reciprocal31.57
I(0) (reciprocal space) i0_reciprocal40790000.0000
Solution quality estimate total_estimate0.7661
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary24.7
Skewness Skewness skewness0.519
Kurtosis Kurtosis kurtosis-0.590
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14770000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.609; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.380; Smooth: 0.747

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)