2efa

Neutron crystal structure of cubic insulin at pD6.6

Method: NEUTRON DIFFRACTION Dmax: 41.6 Å Quality: GOOD

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

Insulin

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 Fragment:Insulin A chain Fragment:Insulin B chain No other associated polymer NEUTRON DIFFRACTION X-ray crystallization conditions:MICRODIALYSIS;pH 6.6;298 K;0.2M Sodium phosphate, 8mM 3NaEDTA, pH 6.6(PD), MICRODIALYSIS, temperature 298K Resolution 2.70 Å R-free 0.291
2 Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 88–108 Chain B; UniProt 25–54 Fragment:Insulin A chain Fragment:Insulin B chain No other associated polymer NEUTRON DIFFRACTION X-ray crystallization conditions:MICRODIALYSIS;pH 6.6;298 K;0.2M Sodium phosphate, 8mM 3NaEDTA, pH 6.6(PD), MICRODIALYSIS, temperature 298K Resolution 2.70 Å R-free 0.291

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 125 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 2efa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2efa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2efa
Deposition date deposition_date2007-02-22
Structure title titleNeutron crystal structure of cubic insulin at pD6.6
Keywords keywordsHORMONE, CUBIC PORCINE INSULIN, HORMONE-GROWTH FACTOR COMPLEX; HORMONE/GROWTH FACTOR
Experimental Method methodNEUTRON DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier12.25
Radius of gyration Rg (electron density) rg_electron10.40
Forward intensity I(0) i01131010.00
Molecular weight molecular_weight6426.0 kDa
Excluded volume excluded_volume7765 ų
Envelope volume envelope_volume9764 ų
Hydration-shell volume shell_volume7959 ų
Envelope diameter envelope_diameter39.6
Shell Rg shell_rg16.18
Envelope Rg envelope_rg11.23
Shape Rg shape_rg10.54
Total Rg total_rg11.73
Total atoms total_atoms829
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 dmax41.6
Rg (real space) rg_real12.21
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.1310e+06
I(0) uncertainty (real space) i0_real_error1.2650e+04
Rg (reciprocal space) rg_reciprocal12.21
I(0) (reciprocal space) i0_reciprocal1131000.0000
Solution quality estimate total_estimate0.8737
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.3
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.191
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha178300.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.794; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2efab1
Class classj — Peptides
Fold Fold foldj.75 — Isolated insulin B-chain
Superfamily Superfamily superfamilyj.75.1 — Isolated insulin B-chain
Family Family familyj.75.1.1 — Isolated insulin B-chain

8. Citations (1)

9. Files and Curves (10)