7a86

rsGreen0.7-K206A-F145L partially in the green-off state

Method: X-RAY DIFFRACTION Dmax: 76.0 Å Quality: GOOD

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

Green fluorescent protein

Aequorea victoria

UniProt A0A059PIQ0

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 3–238 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;293 K;100 mM MES pH 6.5 12 % PEG 20 000 4 % Pentaerythritol ethoxylate Resolution 1.90 Å R-free 0.210
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3–238 Non-standard monomer:Yes (specific site not provided by mmCIF) PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;100 mM MES pH 6.5 12 % PEG 20 000 4 % Pentaerythritol ethoxylate Resolution 1.90 Å R-free 0.210

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.

91 other PDB entries and 136 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A059PIQ0_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 37–270; UniProt 3–238 Author chain B; PDBConstruct 37–270; UniProt 3–238

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 7a86

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7a86
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7a86
Deposition date deposition_date2020-08-30
Structure title titlersGreen0.7-K206A-F145L partially in the green-off state
Keywords keywordsReversible photoswitchable fluorescent 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_guinier23.76
Radius of gyration Rg (electron density) rg_electron22.73
Forward intensity I(0) i043000000.00
Molecular weight molecular_weight50704.0 kDa
Excluded volume excluded_volume63398 ų
Envelope volume envelope_volume74794 ų
Hydration-shell volume shell_volume27059 ų
Envelope diameter envelope_diameter80.0
Shell Rg shell_rg29.81
Envelope Rg envelope_rg22.78
Shape Rg shape_rg22.71
Total Rg total_rg23.59
Total atoms total_atoms3581
Residues n_residues448
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 dmax76.0
Rg (real space) rg_real23.65
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real4.3000e+07
I(0) uncertainty (real space) i0_real_error5.7900e+05
Rg (reciprocal space) rg_reciprocal23.68
I(0) (reciprocal space) i0_reciprocal43000000.0000
Solution quality estimate total_estimate0.8208
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.222
Kurtosis Kurtosis kurtosis-0.449
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11700000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.891; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd7a86a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.22 — GFP-like
Superfamily Superfamily superfamilyd.22.1 — GFP-like
Family Family familyd.22.1.1 — Fluorescent proteins
Domain ID domain_idd7a86b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.22 — GFP-like
Superfamily Superfamily superfamilyd.22.1 — GFP-like
Family Family familyd.22.1.1 — Fluorescent proteins

8. Citations (1)

9. Files and Curves (10)