8z4b

Crystal structure of LysB22-AspB28 insulin analog at ambient structure

Method: X-RAY DIFFRACTION Dmax: 47.5 Å Quality: GOOD

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

Insulin A chain

Homo sapiens

UniProt P01308

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 homooligomer Homooligomer Protein × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain A; UniProt 90–110 Chain B; UniProt 25–54 Chain C; UniProt 90–110 Chain D; UniProt 25–54 Not recorded ZN ZINC ION × 6 CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;2.4 M NaCl, 100 mM Tris-HCl at pH 7.4, 6 mM ZnCI2, 20 (w/v) poly(ethylene glycol) PEG-8000 Resolution 2.50 Å R-free 0.357

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.

369 other PDB entries and 583 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INS_HUMAN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–21; UniProt 90–110 Author chain C; PDBConstruct 1–21; UniProt 90–110 Author chain B; PDBConstruct 1–30; UniProt 25–54 Author chain D; PDBConstruct 1–30; UniProt 25–54

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 8z4b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8z4b
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8z4b
Deposition date deposition_date2024-04-17
Structure title titleCrystal structure of LysB22-AspB28 insulin analog at ambient structure
Keywords keywordsInsulin analog, rapid-acting, HORMONE; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.72
Radius of gyration Rg (electron density) rg_electron13.57
Forward intensity I(0) i02996070.00
Molecular weight molecular_weight11516.0 kDa
Excluded volume excluded_volume14073 ų
Envelope volume envelope_volume16447 ų
Hydration-shell volume shell_volume10664 ų
Envelope diameter envelope_diameter46.3
Shell Rg shell_rg18.80
Envelope Rg envelope_rg13.83
Shape Rg shape_rg13.53
Total Rg total_rg14.76
Total atoms total_atoms793
Residues n_residues102
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 dmax47.5
Rg (real space) rg_real14.66
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real2.9960e+06
I(0) uncertainty (real space) i0_real_error3.2230e+04
Rg (reciprocal space) rg_reciprocal14.67
I(0) (reciprocal space) i0_reciprocal2996000.0000
Solution quality estimate total_estimate0.8898
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.0
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.347
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha364800.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.862; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)