Research workbench
The insulin receptor ectodomain in complex with four venom hybrid insulins - symmetric conformation
Analyse The insulin receptor ectodomain in complex with four venom hybrid insulins… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MQR
- Type
- protein
- Length
- 1,810 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin a chain; Insulin B chain; Isoform short of insulin receptor
- EC
- 2.7.10.1
- UniProt
- P01308, P06213
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 4 distinct chains · 14% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, G, I | Insulin a chain | protein | 24 | 54% helix, 0% strand | P01308 |
| B, D | Insulin B chain | protein | 18 | 50% helix, 0% strand | P01308 |
| E, F | Isoform short of insulin receptor (EC 2.7.10.1) | protein | 823 | 11% helix, 29% strand | P06213 |
| H, J | Insulin B chain | protein | 16 | 50% helix, 0% strand | P01308 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 20 copies · chains E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 821 | 0.78 | 0.81 | 101 | empty |
| 2 | 1155 | 0.77 | 0.79 | 91 | empty |
| 3 | 585 | 0.73 | 0.81 | 66 | empty |
| 4 | 468 | 0.64 | 0.76 | 41 | empty |
| 5 | 449 | 0.63 | 0.77 | 36 | empty |
Interfaces
19 interfaces between chains.
- E–F · 3363 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 491 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 491 Ų buried · 5 hydrogen bonds · protein-protein
- E–C · 440 Ų buried · 0 hydrogen bonds · protein-protein
- A–F · 437 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 48 disulfide, 20 glycan (disulfide, N-glycosylation).
Compared structures
- 7MQR · The insulin receptor ectodomain in complex with four venom hybrid insulins - symmetric… · the same entry in another collection · chain J against J, 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
- Every structure of UniProt P06213
- Elsewhere: RCSB PDB 7MQR · PDBe 7MQR · UniProt P01308 · UniProt P06213
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