6ins

X-RAY ANALYSIS OF THE SINGLE CHAIN B29-A1 PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE

Method: X-RAY DIFFRACTION Dmax: 47.6 Å Quality: GOOD

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

INSULIN

Sus scrofa

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 E; UniProt 25–53 Chain E; UniProt 88–108 Chain F; UniProt 25–53 Chain F; UniProt 88–108 Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 Å
2 Protein homooligomer Homooligomer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 25–53 Chain E; UniProt 88–108 Chain F; UniProt 25–53 Chain F; UniProt 88–108 Not recorded ZN ZINC ION × 6 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.00 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.

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
Chains and sequence ranges Author chain E; PDBConstruct 1–29; UniProt 25–53 Author chain E; PDBConstruct 30–50; UniProt 88–108 Author chain F; PDBConstruct 1–29; UniProt 25–53 Author chain F; PDBConstruct 30–50; UniProt 88–108

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 6ins

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ins
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ins
Deposition date deposition_date1992-11-25
Structure title titleX-RAY ANALYSIS OF THE SINGLE CHAIN B29-A1 PEPTIDE-LINKED INSULIN MOLECULE. A COMPLETELY INACTIVE ANALOGUE
Keywords keywordsHORMONE; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.64
Radius of gyration Rg (electron density) rg_electron13.48
Forward intensity I(0) i02854930.00
Molecular weight molecular_weight11426.0 kDa
Excluded volume excluded_volume14062 ų
Envelope volume envelope_volume16369 ų
Hydration-shell volume shell_volume10624 ų
Envelope diameter envelope_diameter45.5
Shell Rg shell_rg18.83
Envelope Rg envelope_rg13.84
Shape Rg shape_rg13.45
Total Rg total_rg14.71
Total atoms total_atoms790
Residues n_residues100
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 dmax47.6
Rg (real space) rg_real14.59
Rg uncertainty (real space) rg_real_error0.27
I(0) (real space) i0_real2.8550e+06
I(0) uncertainty (real space) i0_real_error3.4750e+04
Rg (reciprocal space) rg_reciprocal14.60
I(0) (reciprocal space) i0_reciprocal2855000.0000
Solution quality estimate total_estimate0.8107
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.7
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha343600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6inse_
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
Domain ID domain_idd6insf_
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

CATH v4.4 (2 domains)

Domain ID domain_id6insE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like
Domain ID domain_id6insF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology100 — Insulin-like, subunit E
Homologous superfamily homologous superfamily10 — Insulin-like

8. Citations (2)

9. Files and Curves (10)