1b18

PH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 5.53 COORDINATES)

Method: X-RAY DIFFRACTION Dmax: 36.0 Å Quality: GOOD

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

PROTEIN (INSULIN a chain)

OrganismNot specified

UniProt P01315

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 88–108 Chain B; UniProt 25–54 Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.53;pH 5.53 Resolution 1.80 Å R-free 0.216
2 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 88–108 Chain B; UniProt 25–54 Not recorded SO4 SULFATE ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.53;pH 5.53 Resolution 1.80 Å R-free 0.216
3 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 88–108 Chain B; UniProt 25–54 Not recorded SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.53;pH 5.53 Resolution 1.80 Å R-free 0.216

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.

41 other PDB entries and 124 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INS_PIG
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–21; UniProt 88–108 Author chain B; 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 1b18

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1b18
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1b18
Deposition date deposition_date1998-11-26
Structure title titlePH AFFECTS GLU B13 SWITCHING AND SULFATE BINDING IN CUBIC INSULIN CRYSTALS (PH 5.53 COORDINATES)
Keywords keywordsHORMONE, GLUCOSE CONCENTRATION DECREASE, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier11.42
Radius of gyration Rg (electron density) rg_electron9.98
Forward intensity I(0) i0877354.00
Molecular weight molecular_weight5878.0 kDa
Excluded volume excluded_volume7230 ų
Envelope volume envelope_volume7933 ų
Hydration-shell volume shell_volume7073 ų
Envelope diameter envelope_diameter33.1
Shell Rg shell_rg15.17
Envelope Rg envelope_rg10.31
Shape Rg shape_rg9.98
Total Rg total_rg11.44
Total atoms total_atoms408
Residues n_residues51
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 dmax36.0
Rg (real space) rg_real11.35
Rg uncertainty (real space) rg_real_error0.19
I(0) (real space) i0_real8.7740e+05
I(0) uncertainty (real space) i0_real_error8.7990e+03
Rg (reciprocal space) rg_reciprocal11.35
I(0) (reciprocal space) i0_reciprocal877400.0000
Solution quality estimate total_estimate0.8982
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.1
Skewness Skewness skewness0.098
Kurtosis Kurtosis kurtosis-0.352
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha86550.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.987

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1b18.1
Class classg — Small proteins
Fold Fold foldg.1 — Insulin-like
Superfamily Superfamily superfamilyg.1.1 — Insulin-like
Family Family familyg.1.1.1 — Insulin-like

8. Citations (7)

9. Files and Curves (10)