Research workbench
Insulin in complex with site 1 of the human insulin receptor
Analyse Insulin in complex with site 1 of the human insulin receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OGA
- Type
- protein
- Length
- 577 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a chain; Insulin B chain; Monoclonal antibody Fab 83-7 fragment - heavy chain…
- UniProt
- P01308, P06213
- Ligands
- NAG, BMA, MAN, FUC
- Pockets
- 5 · best druggability 0.48
Structure
x-ray diffraction · 6 distinct chains · 12% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin a chain | protein | 21 | 24% helix, 5% strand | P01308 |
| B | Insulin B chain | protein | 21 | 62% helix, 5% strand | P01308 |
| C | Monoclonal antibody Fab 83-7 fragment - heavy chain | protein | 118 | 8% helix, 48% strand | — |
| D | Monoclonal antibody Fab 83-7 fragment - light chain | protein | 114 | 5% helix, 54% strand | — |
| E | Insulin receptor domains L1-cr | protein | 288 | 10% helix, 32% strand | P06213 |
| F | Insulin receptor alpha-ct peptide | protein | 15 | 53% helix, 0% strand | P06213 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains E, C, B
- BMA · beta-D-mannopyranose · sugar · 2 copies
- MAN · alpha-D-mannopyranose · sugar · chains E
- FUC · alpha-L-fucopyranose · sugar · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.48 | 0.78 | 31 | NAG |
| 2 | 133 | 0.44 | 0.77 | 26 | empty |
| 3 | 105 | 0.41 | 0.77 | 23 | empty |
| 4 | 101 | 0.37 | 0.74 | 17 | empty |
| 5 | 61 | 0.25 | 0.72 | 25 | empty |
Interfaces
8 interfaces between chains.
- C–D · 851 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 509 Ų buried · 3 hydrogen bonds · protein-protein
- C–E · 489 Ų buried · 9 hydrogen bonds · protein-protein
- B–E · 474 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 440 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide, 5 glycan (disulfide, N-glycosylation).
Compared structures
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
- Every structure of UniProt P06213
- Elsewhere: RCSB PDB 4OGA · PDBe 4OGA · UniProt P01308 · UniProt P06213
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