3ekh

Calcium-saturated GCaMP2 T116V/K378W mutant monomer

Method: X-RAY DIFFRACTION Dmax: 81.4 Å Quality: GOOD

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

Myosin light chain kinase, Green fluorescent protein, Calmodulin chimera

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 3–149 Mutation:T116V, K378W Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;0.1 M Magnesium formate dihydrate, 15% w/v Polyethylene glycol 3,350, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.224

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 303–449; UniProt 3–149

Myosin light chain kinase, Green fluorescent protein, Calmodulin chimera

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 Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 149–238 Chain A; UniProt 2–144 Mutation:T116V, K378W Non-standard monomer:Yes (specific site not provided by mmCIF) GOL GLYCEROL × 1 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;298 K;0.1 M Magnesium formate dihydrate, 15% w/v Polyethylene glycol 3,350, pH 8, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.00 Å R-free 0.224

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 62–151; UniProt 149–238 Author chain A; PDBConstruct 160–300; UniProt 2–144

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 3ekh

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3ekh
Deposition date deposition_date2008-09-19
Structure title titleCalcium-saturated GCaMP2 T116V/K378W mutant monomer
Keywords keywordsGECI, GCaMP2, cpEGFP, calmodulin, M13 peptide, SIGNALING PROTEIN, 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_guinier23.71
Radius of gyration Rg (electron density) rg_electron22.69
Forward intensity I(0) i035517400.00
Molecular weight molecular_weight45048.0 kDa
Excluded volume excluded_volume55959 ų
Envelope volume envelope_volume66616 ų
Hydration-shell volume shell_volume24738 ų
Envelope diameter envelope_diameter79.0
Shell Rg shell_rg29.47
Envelope Rg envelope_rg22.77
Shape Rg shape_rg22.66
Total Rg total_rg23.58
Total atoms total_atoms3162
Residues n_residues394
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 dmax81.4
Rg (real space) rg_real23.68
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real3.5520e+07
I(0) uncertainty (real space) i0_real_error4.8620e+05
Rg (reciprocal space) rg_reciprocal23.69
I(0) (reciprocal space) i0_reciprocal35520000.0000
Solution quality estimate total_estimate0.8765
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.7
Skewness Skewness skewness0.313
Kurtosis Kurtosis kurtosis-0.402
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha8642000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.809; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.965; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3ekhA01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id3ekhA02
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein

8. Citations (2)

9. Files and Curves (10)