1mso

T6 Human Insulin at 1.0 A Resolution

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

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

Insulin A-Chain

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 25–54 Chain C; UniProt 90–110 Chain D; UniProt 25–54 Not recorded ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:SLOW COOLING;pH 6.3;298 K;0.001 M HCl, 0.007 M Zinc Acetate, 0.05 M Sodium Citrate, 17% acetone, pH 6.3, SLOW COOLING at 298K, temperature 298.0K Resolution 1.00 Å R-free 0.201

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 1mso

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1mso
Deposition date deposition_date2002-09-19
Structure title titleT6 Human Insulin at 1.0 A Resolution
Keywords keywordsT6 Conformation, 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_guinier14.87
Radius of gyration Rg (electron density) rg_electron13.71
Forward intensity I(0) i03004870.00
Molecular weight molecular_weight11677.0 kDa
Excluded volume excluded_volume14361 ų
Envelope volume envelope_volume16370 ų
Hydration-shell volume shell_volume10532 ų
Envelope diameter envelope_diameter49.9
Shell Rg shell_rg19.00
Envelope Rg envelope_rg14.19
Shape Rg shape_rg13.67
Total Rg total_rg14.94
Total atoms total_atoms1565
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 dmax51.0
Rg (real space) rg_real14.84
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real3.0050e+06
I(0) uncertainty (real space) i0_real_error3.0190e+04
Rg (reciprocal space) rg_reciprocal14.84
I(0) (reciprocal space) i0_reciprocal3005000.0000
Solution quality estimate total_estimate0.8642
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.1
Skewness Skewness skewness0.291
Kurtosis Kurtosis kurtosis-0.239
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha335400.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.756; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.980

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1mso.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
Domain ID domain_idd1mso.2
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 (1)

9. Files and Curves (10)