1htv

CRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN

Method: X-RAY DIFFRACTION Dmax: 57.6 Å Quality: EXCELLENT

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

INSULIN

Homo sapiens

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 25–51 Chain C; UniProt 90–110 Chain D; UniProt 25–51 Chain E; UniProt 90–110 Chain F; UniProt 25–51 Chain G; UniProt 90–110 Chain H; UniProt 25–51 Chain I; UniProt 90–110 Chain J; UniProt 25–51 Chain K; UniProt 90–110 Chain L; UniProt 25–51 Fragment:INSULIN A CHAIN Fragment:INSULIN B CHAIN ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;298 K;sodium citrate, dimethylformamide, zinc acetate, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 1.90 Å R-free 0.240

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 E; PDBConstruct 1–21; UniProt 90–110 Author chain G; PDBConstruct 1–21; UniProt 90–110 Author chain I; PDBConstruct 1–21; UniProt 90–110 Author chain K; PDBConstruct 1–21; UniProt 90–110 Author chain B; PDBConstruct 1–27; UniProt 25–51 Author chain D; PDBConstruct 1–27; UniProt 25–51 Author chain F; PDBConstruct 1–27; UniProt 25–51 Author chain H; PDBConstruct 1–27; UniProt 25–51 Author chain J; PDBConstruct 1–27; UniProt 25–51 Author chain L; PDBConstruct 1–27; UniProt 25–51

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 1htv

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1htv
Deposition date deposition_date2001-01-01
Structure title titleCRYSTAL STRUCTURE OF DESTRIPEPTIDE (B28-B30) INSULIN
Keywords keywordsHELIX, BETA SHEET, 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_guinier20.03
Radius of gyration Rg (electron density) rg_electron18.92
Forward intensity I(0) i019474300.00
Molecular weight molecular_weight32869.0 kDa
Excluded volume excluded_volume40616 ų
Envelope volume envelope_volume47634 ų
Hydration-shell volume shell_volume20680 ų
Envelope diameter envelope_diameter58.3
Shell Rg shell_rg25.46
Envelope Rg envelope_rg18.77
Shape Rg shape_rg18.93
Total Rg total_rg19.73
Total atoms total_atoms2287
Residues n_residues288
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 dmax57.6
Rg (real space) rg_real19.86
Rg uncertainty (real space) rg_real_error0.21
I(0) (real space) i0_real1.9470e+07
I(0) uncertainty (real space) i0_real_error2.2480e+05
Rg (reciprocal space) rg_reciprocal19.89
I(0) (reciprocal space) i0_reciprocal19470000.0000
Solution quality estimate total_estimate0.9081
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.5
Skewness Skewness skewness-0.019
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2558000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.963; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (6 domains)

Domain ID domain_idd1htv.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_idd1htv.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
Domain ID domain_idd1htv.3
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_idd1htv.4
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_idd1htv.5
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_idd1htv.6
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 (3)

9. Files and Curves (10)