Research workbench
R6 human insulin hexamer (symmetric), NMR, 20 structures
Analyse R6 human insulin hexamer (symmetric), NMR, 20 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AIY
- Type
- protein
- Length
- 306 residues
- Chains
- 12
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (insulin)
- UniProt
- P01308
- Ligands
- IPH
- Pockets
- 8 · best druggability 0.71
Structure
solution nmr · 2 distinct chains · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Protein (insulin) | protein | 21 | 67% helix, 5% strand | P01308 |
| B, D, F, H, J, L | Protein (insulin) | protein | 30 | 53% helix, 10% strand | P01308 |
Ligands and binding sites
- IPH · Phenol · ligand · 6 copies · chains A, B, F, H, C, D, J, L, E, G, I, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 165 | 0.71 | 0.89 | 27 | empty |
| 2 | 62 | 0.69 | 0.96 | 18 | empty |
| 3 | 182 | 0.68 | 0.87 | 24 | empty |
| 4 | 62 | 0.68 | 0.95 | 18 | empty |
| 5 | 215 | 0.66 | 0.83 | 34 | IPH |
Interfaces
30 interfaces between chains.
- B–D · 822 Ų buried · 14 hydrogen bonds · protein-protein
- F–H · 820 Ų buried · 14 hydrogen bonds · protein-protein
- J–L · 816 Ų buried · 14 hydrogen bonds · protein-protein
- I–J · 637 Ų buried · 8 hydrogen bonds · protein-protein
- K–L · 636 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide (disulfide).
Compared structures
- 2AIY · R6 human insulin hexamer (symmetric), NMR, 20 structures · 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 2AIY · PDBe 2AIY · UniProt P01308
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