Research workbench
Insulin lispro analog
Analyse Insulin lispro analog in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NWV
- Type
- protein
- Length
- 295 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a chain; Insulin lispro B chain
- UniProt
- P01308
- Ligands
- CRS, ZN, CL
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 5 distinct chains · 69% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Insulin a chain | protein | 21 | 57% helix, 5% strand | P01308 |
| B | Insulin lispro B chain | protein | 27 | 70% helix, 11% strand | P01308 |
| D | Insulin lispro B chain | protein | 29 | 72% helix, 10% strand | P01308 |
| F, H, L | Insulin lispro B chain | protein | 29 | 72% helix, 10% strand | P01308 |
| J | Insulin lispro B chain | protein | 26 | 69% helix, 12% strand | P01308 |
Ligands and binding sites
- CRS · M-cresol · ligand · 7 copies · chains A, B, D, F, C, J, L, E, H, G, K, I
- ZN · Zinc ion · metal · 2 copies · chains B, D, L, F, H, J
- CL · Chloride ion · ion · 2 copies · chains F, H, J, B, D, L
- GOL · Glycerol · additive · 2 copies · chains C, D, L, A, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 278 | 0.80 | 0.92 | 55 | CRS |
| 2 | 247 | 0.76 | 0.89 | 45 | CRS, GOL |
| 3 | 481 | 0.76 | 0.84 | 77 | CRS, CL |
| 4 | 123 | 0.47 | 0.79 | 23 | GOL, CL |
| 5 | 58 | 0.33 | 0.76 | 16 | empty |
Interfaces
39 interfaces between chains.
- B–H · 759 Ų buried · 11 hydrogen bonds · protein-protein
- J–L · 744 Ų buried · 15 hydrogen bonds · protein-protein
- D–F · 737 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 551 Ų buried · 4 hydrogen bonds · protein-protein
- E–F · 549 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide (disulfide).
Compared structures
- 6NWV · Insulin Lispro Analog · 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 6NWV · PDBe 6NWV · UniProt P01308
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