1uz9

Crystallographic and solution studies of N-lithocholyl insulin: a new generation of prolonged-acting insulins.

Method: X-RAY DIFFRACTION Dmax: 51.0 Å Quality: REASONABLE

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

INSULIN

OrganismNot specified

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: dodecameric(12) Consistent with protein copy count Chain A; UniProt 90–110 Chain B; UniProt 25–53 Fragment:INSULIN A CHAIN, RESIDUES 90-110 Fragment:INSULIN B CHAIN, RESIDUES 25-53 CRS M-CRESOL × 6 UZ9 (2S)-2-AMINO-6-({(4R)-4-[(10R,13S)-10,13-DIMETHYL-3-OXOHEXADECAHYDRO-1H-CYCLOPENTA[A]PHENANTHREN-17-YL]PENTANOYL}AMINO)HEXANOIC ACID × 6 ZN ZINC ION × 6 CL CHLORIDE ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:pH 8;0.5 M TRIS-HCL PH 8.0 0.1M TRI-SODIUM CITRATE, 2MM ZINC ACETATE, 0.05% W/V M-CRESOL Resolution 1.60 Å R-free 0.206

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 B; PDBConstruct 1–29; UniProt 25–53

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 1uz9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1uz9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1uz9
Deposition date deposition_date2004-03-08
Structure title titleCrystallographic and solution studies of N-lithocholyl insulin: a new generation of prolonged-acting insulins.
Keywords keywordsINSULIN, DIABETES MELLITUS, INSULIN FAMILY, HORMONE DISEASE MUTATION; INSULIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier12.17
Radius of gyration Rg (electron density) rg_electron11.54
Forward intensity I(0) i0899032.00
Molecular weight molecular_weight6276.0 kDa
Excluded volume excluded_volume7906 ų
Envelope volume envelope_volume9102 ų
Hydration-shell volume shell_volume7335 ų
Envelope diameter envelope_diameter47.8
Shell Rg shell_rg16.30
Envelope Rg envelope_rg12.07
Shape Rg shape_rg11.55
Total Rg total_rg12.91
Total atoms total_atoms434
Residues n_residues49
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 dmax51.0
Rg (real space) rg_real12.18
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real8.9900e+05
I(0) uncertainty (real space) i0_real_error1.0420e+04
Rg (reciprocal space) rg_reciprocal12.18
I(0) (reciprocal space) i0_reciprocal899000.0000
Solution quality estimate total_estimate0.7469
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.8
Skewness Skewness skewness0.398
Kurtosis Kurtosis kurtosis0.209
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha101500.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.370; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.595; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)