5bt0

Switching GFP fluorescence using genetically encoded phenyl azide chemistry through two different non-native post-translational modifications routes at the same position.

Method: X-RAY DIFFRACTION Dmax: 85.1 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 3–234 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;297 K;50 mM MMT, 2.5 M (NH4)2SO4 Resolution 2.03 Å R-free 0.204
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 3–234 Non-standard monomer:Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;297 K;50 mM MMT, 2.5 M (NH4)2SO4 Resolution 2.03 Å R-free 0.204

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 2–231; UniProt 3–234 Author chain B; PDBConstruct 2–231; UniProt 3–234

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 5bt0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5bt0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5bt0
Deposition date deposition_date2015-06-02
Structure title titleSwitching GFP fluorescence using genetically encoded phenyl azide chemistry through two different non-native post-translational modifications routes at the same position.
Keywords keywordssynthetic biology, photocontrol, optogenetics, unnatural amino acids, protein fluorescence, sfGFP, 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_guinier26.00
Radius of gyration Rg (electron density) rg_electron25.23
Forward intensity I(0) i048332200.00
Molecular weight molecular_weight52719.0 kDa
Excluded volume excluded_volume65468 ų
Envelope volume envelope_volume79152 ų
Hydration-shell volume shell_volume26722 ų
Envelope diameter envelope_diameter91.3
Shell Rg shell_rg31.73
Envelope Rg envelope_rg25.29
Shape Rg shape_rg25.20
Total Rg total_rg26.06
Total atoms total_atoms3710
Residues n_residues458
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 dmax85.1
Rg (real space) rg_real26.05
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real4.8330e+07
I(0) uncertainty (real space) i0_real_error7.0620e+05
Rg (reciprocal space) rg_reciprocal26.04
I(0) (reciprocal space) i0_reciprocal48330000.0000
Solution quality estimate total_estimate0.8838
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.423
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13700000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd5bt0a1
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_idd5bt0a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5bt0b1
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_idd5bt0b2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id5bt0A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id5bt0B00
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)