1pid

BOVINE DESPENTAPEPTIDE INSULIN

Method: X-RAY DIFFRACTION Dmax: 53.9 Å Quality: GOOD

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

DESPENTAPEPTIDE INSULIN

OrganismNot specified

UniProt P01317

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 85–105 Chain B; UniProt 25–49 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.30 Å
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 85–105 Chain D; UniProt 25–49 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.30 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.

39 other PDB entries and 85 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INS_BOVIN
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–21; UniProt 85–105 Author chain C; PDBConstruct 1–21; UniProt 85–105 Author chain B; PDBConstruct 1–25; UniProt 25–49 Author chain D; PDBConstruct 1–25; UniProt 25–49

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 1pid

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1pid
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1pid
Deposition date deposition_date1995-11-22
Structure title titleBOVINE DESPENTAPEPTIDE INSULIN
Keywords keywordsHORMONE, GLUCOSE METABOLISM; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier17.46
Radius of gyration Rg (electron density) rg_electron16.86
Forward intensity I(0) i02329720.00
Molecular weight molecular_weight10352.0 kDa
Excluded volume excluded_volume12754 ų
Envelope volume envelope_volume17103 ų
Hydration-shell volume shell_volume9241 ų
Envelope diameter envelope_diameter52.9
Shell Rg shell_rg21.01
Envelope Rg envelope_rg16.62
Shape Rg shape_rg16.89
Total Rg total_rg17.61
Total atoms total_atoms720
Residues n_residues92
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 dmax53.9
Rg (real space) rg_real17.49
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.3300e+06
I(0) uncertainty (real space) i0_real_error2.8610e+04
Rg (reciprocal space) rg_reciprocal17.49
I(0) (reciprocal space) i0_reciprocal2330000.0000
Solution quality estimate total_estimate0.8281
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary15.8
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.756
Angular range angular_range— – 0.4550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha157400.0000
Real-space data points n_real_points76
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.891; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1pid.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_idd1pid.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 (2)

9. Files and Curves (10)