Research workbench
Crystal structure of dodecamer human insulin with double C-axis length of the hexamer 2 zn insulin cell
Analyse Crystal structure of dodecamer human insulin with double C-axis length of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3W80
- Type
- protein
- Length
- 204 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin
- UniProt
- P01308
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Insulin | protein | 21 | 67% helix, 10% strand | P01308 |
| B, D, F, H | Insulin | protein | 30 | 47% helix, 13% strand | P01308 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains B, D, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 237 | 0.52 | 0.76 | 33 | empty |
Interfaces
14 interfaces between chains.
- A–B · 896 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 895 Ų buried · 15 hydrogen bonds · protein-protein
- G–H · 838 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 837 Ų buried · 10 hydrogen bonds · protein-protein
- F–H · 669 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 3W80 · Crystal structure of dodecamer human insulin with double C-axis length of the hexamer 2… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01308
- Elsewhere: RCSB PDB 3W80 · PDBe 3W80 · UniProt P01308
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