9u9d

Bipartite Genetically Encoded Biosensor sG-GECO1

Method: X-RAY DIFFRACTION Dmax: 59.3 Å Quality: REASONABLE

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

Myosin light chain kinase, smooth muscle, deglutamylated form,Green fluorescent protein,Calmodulin-1

Rattus norvegicus

UniProt P0DP29

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 Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 3–149 Not recorded Green fluorescent protein × 1 (P42212) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2m sodium malonate dibasic monohydrate, 0.1M Bis-Tris propane pH 8.5, 20% w/v PEG 3350 Resolution 1.80 Å R-free 0.227

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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 88–234; UniProt 3–149

Myosin light chain kinase, smooth muscle, deglutamylated form,Green fluorescent protein,Calmodulin-1

Rattus norvegicus

UniProt P11799

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 Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1726–1749 Not recorded Green fluorescent protein × 1 (P42212) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.2m sodium malonate dibasic monohydrate, 0.1M Bis-Tris propane pH 8.5, 20% w/v PEG 3350 Resolution 1.80 Å R-free 0.227

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.

6 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYLK_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 37–60; UniProt 1726–1749

Myosin light chain kinase, smooth muscle, deglutamylated form,Green fluorescent protein,Calmodulin-1

Rattus norvegicus

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 Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 149–172 Chain B; UniProt 170–238 Chain B; UniProt 2–146 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;293 K;0.2m sodium malonate dibasic monohydrate, 0.1M Bis-Tris propane pH 8.5, 20% w/v PEG 3350 Resolution 1.80 Å R-free 0.227

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, 2
Chains and sequence ranges Author chain A; PDBConstruct 61–84; UniProt 149–172 Author chain B; PDBConstruct 13–81; UniProt 170–238 Author chain B; PDBConstruct 90–232; 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 9u9d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9u9d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9u9d
Deposition date deposition_date2025-03-27
Structure title titleBipartite Genetically Encoded Biosensor sG-GECO1
Keywords keywordsFluorescent protein, GFP, bipartite scpFP, sG-GECO1; FLUORESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.42
Radius of gyration Rg (electron density) rg_electron17.16
Forward intensity I(0) i012100200.00
Molecular weight molecular_weight26058.0 kDa
Excluded volume excluded_volume32671 ų
Envelope volume envelope_volume36697 ų
Hydration-shell volume shell_volume17732 ų
Envelope diameter envelope_diameter60.7
Shell Rg shell_rg23.58
Envelope Rg envelope_rg17.60
Shape Rg shape_rg17.14
Total Rg total_rg18.24
Total atoms total_atoms1839
Residues n_residues230
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 dmax59.3
Rg (real space) rg_real18.33
Rg uncertainty (real space) rg_real_error0.22
I(0) (real space) i0_real1.2100e+07
I(0) uncertainty (real space) i0_real_error1.3740e+05
Rg (reciprocal space) rg_reciprocal18.34
I(0) (reciprocal space) i0_reciprocal12100000.0000
Solution quality estimate total_estimate0.6579
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.6
Skewness Skewness skewness0.228
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0046
Highest regularization parameter α highest_alpha4130000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 0.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)