28ql

GFP bound to distal DARPin (AHIR dodecamer scaffold system)

Method: ELECTRON MICROSCOPY Dmax: 71.7 Å Quality: EXCELLENT

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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 3–229 Not recorded DARPin × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.72 Å

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 137 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A059PIQ0_AEQVI
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–227; UniProt 3–229

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 28ql

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 28ql
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2. Structure Basics 2. Structure Basics

Entry ID entry_id28ql
Deposition date deposition_date2026-02-13
Structure title titleGFP bound to distal DARPin (AHIR dodecamer scaffold system)
Keywords keywordsGFP, DARPin, scaffold, FLUORESCENT PROTEIN; FLUORESCENT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier22.51
Radius of gyration Rg (electron density) rg_electron21.56
Forward intensity I(0) i031374300.00
Molecular weight molecular_weight42839.0 kDa
Excluded volume excluded_volume53574 ų
Envelope volume envelope_volume62900 ų
Hydration-shell volume shell_volume24232 ų
Envelope diameter envelope_diameter71.1
Shell Rg shell_rg28.50
Envelope Rg envelope_rg21.85
Shape Rg shape_rg21.52
Total Rg total_rg22.52
Total atoms total_atoms3025
Residues n_residues388
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 dmax71.7
Rg (real space) rg_real22.41
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real3.1370e+07
I(0) uncertainty (real space) i0_real_error3.9700e+05
Rg (reciprocal space) rg_reciprocal22.44
I(0) (reciprocal space) i0_reciprocal31370000.0000
Solution quality estimate total_estimate0.9021
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.1
Skewness Skewness skewness0.193
Kurtosis Kurtosis kurtosis-0.492
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha11480000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.912; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)