2o24

Spectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-Cl Complex

Method: X-RAY DIFFRACTION Dmax: 64.7 Å Quality: GOOD

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 2–238 Mutation:F64L, T203Y, H231L Non-standard monomer:Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;14% (W/V) PEG 3350, 100 MM NH4 ACETATE, 0.2 M NH4CL, PH 5.0, VAPOR DIFFUSION, HANGING DROP Resolution 1.45 Å R-free 0.192

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 8–242; UniProt 2–238

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 2o24

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2o24
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2o24
Deposition date deposition_date2006-11-29
Structure title titleSpectroscopic and Structural Study of the Heterotropic Linkage between Halide and Proton Ion Binding to Gfp Proteins: E2(GFP)-Cl Complex
Keywords keywords;LUMINESCENCE, GREEN FLUORESCENT PROTEIN, GFP, E2, BIOLUMINESCENCE, PHOTOACTIVE PROTEIN, FLUORESCENT CHLORIDE, BROMIDE, IODINE, HALOGEN, LUMINESCENT PROTEIN ;; LUMINESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.86
Radius of gyration Rg (electron density) rg_electron17.70
Forward intensity I(0) i012944500.00
Molecular weight molecular_weight26962.0 kDa
Excluded volume excluded_volume33756 ų
Envelope volume envelope_volume38885 ų
Hydration-shell volume shell_volume18217 ų
Envelope diameter envelope_diameter66.5
Shell Rg shell_rg24.23
Envelope Rg envelope_rg18.49
Shape Rg shape_rg17.70
Total Rg total_rg18.73
Total atoms total_atoms1901
Residues n_residues236
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 dmax64.7
Rg (real space) rg_real18.80
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.2940e+07
I(0) uncertainty (real space) i0_real_error1.6010e+05
Rg (reciprocal space) rg_reciprocal18.81
I(0) (reciprocal space) i0_reciprocal12940000.0000
Solution quality estimate total_estimate0.7814
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.2
Skewness Skewness skewness0.322
Kurtosis Kurtosis kurtosis-0.152
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4541000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.721; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2o24a1
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_idd2o24a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2o24A00
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)