Research workbench
Insulin receptor (domains 1-3)
Analyse Insulin receptor (domains 1-3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HR7
- Type
- protein
- Length
- 929 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin receptor
- EC
- 2.7.1.112
- UniProt
- P06213
- Ligands
- NAG, MAN, BMA, FUC, SO4
- Pockets
- 13 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin receptor (EC 2.7.1.112) | protein | 465 | 12% helix, 30% strand | P06213 |
| B | Insulin receptor (EC 2.7.1.112) | protein | 464 | 13% helix, 29% strand | P06213 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 26 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 10 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 6 copies
- FUC · alpha-L-fucopyranose · sugar · 6 copies · chains A, B
- SO4 · Sulfate ion · ion · 8 copies · chains A, B
- GOL · Glycerol · additive · 19 copies · chains A, B
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.76 | 0.91 | 28 | P33 |
| 2 | 309 | 0.56 | 0.76 | 28 | empty |
| 3 | 388 | 0.55 | 0.74 | 43 | GOL |
| 4 | 130 | 0.54 | 0.82 | 27 | NAG |
| 5 | 148 | 0.53 | 0.80 | 27 | GOL |
Interfaces
1 interface between chains.
- A–B · 1811 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 disulfide, 15 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 P06213
- Elsewhere: RCSB PDB 2HR7 · PDBe 2HR7 · UniProt P06213
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