3ss0

Engineered high-affinity halide-binding protein derived from YFP: fluoride complex

Method: X-RAY DIFFRACTION Dmax: 63.1 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 1–238 Mutation:S72A, K79R, Q183A, T203Y, H231L Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.6;290 K;17% PEG3000, 100 mM sodium acetate, 90 mM magnesium chloride, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K Resolution 1.49 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 1–237; UniProt 1–238

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 3ss0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3ss0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3ss0
Deposition date deposition_date2011-07-07
Structure title titleEngineered high-affinity halide-binding protein derived from YFP: fluoride complex
Keywords keywordsbeta barrel, luminescent protein, yellow fluorescent protein, imaging reagent, HALIDE BINDING PROTEIN; HALIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.76
Radius of gyration Rg (electron density) rg_electron17.47
Forward intensity I(0) i012297200.00
Molecular weight molecular_weight26302.0 kDa
Excluded volume excluded_volume32960 ų
Envelope volume envelope_volume38101 ų
Hydration-shell volume shell_volume18054 ų
Envelope diameter envelope_diameter62.9
Shell Rg shell_rg24.13
Envelope Rg envelope_rg18.16
Shape Rg shape_rg17.44
Total Rg total_rg18.63
Total atoms total_atoms3665
Residues n_residues231
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 dmax63.1
Rg (real space) rg_real18.70
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.2300e+07
I(0) uncertainty (real space) i0_real_error1.6690e+05
Rg (reciprocal space) rg_reciprocal18.71
I(0) (reciprocal space) i0_reciprocal12300000.0000
Solution quality estimate total_estimate0.7918
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.199
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3897000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.763; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd3ss0a_
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 (1 domains)

Domain ID domain_id3ss0A00
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)