1gfl

STRUCTURE OF GREEN FLUORESCENT PROTEIN

Method: X-RAY DIFFRACTION Dmax: 71.2 Å Quality: REASONABLE

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

GREEN FLUORESCENT PROTEIN

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2–239 Mutation:Q80R No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;FREE TEXT GOES HERE., pH 7.0 Resolution 1.90 Å R-free 0.262
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 2–239 Mutation:Q80R No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 7;FREE TEXT GOES HERE., pH 7.0 Resolution 1.90 Å R-free 0.262

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 743 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 1–238; UniProt 2–239 Author chain B; PDBConstruct 1–238; UniProt 2–239

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 1gfl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1gfl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1gfl
Deposition date deposition_date1996-08-23
Structure title titleSTRUCTURE OF GREEN FLUORESCENT PROTEIN
Keywords keywordsFLUOROPHORE GREEN FLUORESCENT PROTEIN, LUMINESCENCE, 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_guinier23.75
Radius of gyration Rg (electron density) rg_electron22.65
Forward intensity I(0) i044459000.00
Molecular weight molecular_weight51682.0 kDa
Excluded volume excluded_volume64682 ų
Envelope volume envelope_volume75363 ų
Hydration-shell volume shell_volume27239 ų
Envelope diameter envelope_diameter78.7
Shell Rg shell_rg29.91
Envelope Rg envelope_rg22.78
Shape Rg shape_rg22.62
Total Rg total_rg23.60
Total atoms total_atoms3650
Residues n_residues460
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 dmax71.2
Rg (real space) rg_real23.72
Rg uncertainty (real space) rg_real_error0.13
I(0) (real space) i0_real4.3120e+07
I(0) uncertainty (real space) i0_real_error4.2310e+05
Rg (reciprocal space) rg_reciprocal23.67
I(0) (reciprocal space) i0_reciprocal44460000.0000
Solution quality estimate total_estimate0.7077
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary27.8
Skewness Skewness skewness0.226
Kurtosis Kurtosis kurtosis-0.458
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha7.8100
Highest regularization parameter α highest_alpha11460000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 0.921; Sysdev: 0.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.562

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1gfla_
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_idd1gflb_
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

CATH v4.4 (2 domains)

Domain ID domain_id1gflA00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology155 — Green Fluorescent Protein
Homologous superfamily homologous superfamily10 — Green fluorescent protein
Domain ID domain_id1gflB00
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)