Download MendeleyStructure of insulin in 4-zinc insulin.
Bentley, G., Dodson, E., Dodson, G., Hodgkin, D., Mercola, D.(1976) Nature 261: 166-168
- PubMed: 1272390
- DOI: https://doi.org/10.1038/261166a0
- Primary Citation of Related Structures:
1ZNI
1ZNI
INSULIN
- PDB DOI: https://doi.org/10.2210/pdb1ZNI/pdb
- Classification: HORMONE
- Organism(s): Sus scrofa
- Mutation(s): No
- Deposited: 1997-09-23 Released: 1998-01-28
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Work: 0.178
wwPDB Validation 3D Report Full Report
This is version 1.4 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by: Sequence | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| INSULIN | 21 | Sus scrofa | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for P01315 (Sus scrofa) Explore P01315 Go to UniProtKB: P01315 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P01315 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| INSULIN | 30 | Sus scrofa | Mutation(s): 0 |  | |
UniProt | |||||
Find proteins for P01315 (Sus scrofa) Explore P01315 Go to UniProtKB: P01315 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P01315 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ZN Query on ZN | E [auth B], F [auth B], J [auth D] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| CL Query on CL | G [auth B], H [auth B], I [auth B] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Work: 0.178
- Space Group: H 3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 80.7 | α = 90 |
| b = 80.7 | β = 90 |
| c = 37.6 | γ = 120 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
Entry History
Deposition Data
- Released Date: 1998-01-28 Deposition Author(s): Turkenburg, M.G.W., Whittingham, J.L., Dodson, G.G., Dodson, E.J., Xiao, B., Bentley, G.A.
Revision History (Full details and data files)
- Version 1.0: 1998-01-28
Type: Initial release - Version 1.1: 2008-03-03
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2017-11-29
Changes: Derived calculations, Other - Version 1.4: 2018-07-04
Changes: Advisory, Data collection, Derived calculations
