Research workbench
Crystal structure of the insulin receptor kinase in complex with the SH2 domain of aps
Analyse Crystal structure of the insulin receptor kinase in complex with the SH2 domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1RQQ
- Type
- protein
- Length
- 787 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin receptor; Adaptor protein aps; Bisubstrate inhibitor
- EC
- 2.7.1.112
- UniProt
- P06213, Q9Z200
- Ligands
- 112, MN
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 4 distinct chains · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Insulin receptor (EC 2.7.1.112) | protein | 297 | 35% helix, 19% strand | P06213 |
| C, D | Adaptor protein aps | protein | 83 | 37% helix, 24% strand | Q9Z200 |
| E | Bisubstrate inhibitor | protein | 14 | 21% helix, 21% strand | — |
| F | Bisubstrate inhibitor | protein | 13 | 23% helix, 23% strand | — |
Ligands and binding sites
- 112 · Thiophosphoric acid O-((adenosyl-phospho)phospho)-S-acetamidyl-diester · ligand · 2 copies · chains A, E, B, F
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 616 | 0.78 | 0.83 | 58 | MN, 112 |
| 2 | 649 | 0.75 | 0.81 | 50 | MN, 112 |
| 3 | 644 | 0.68 | 0.77 | 60 | empty |
| 4 | 99 | 0.46 | 0.79 | 22 | empty |
| 5 | 87 | 0.30 | 0.72 | 17 | empty |
Interfaces
7 interfaces between chains.
- C–D · 949 Ų buried · 2 hydrogen bonds · protein-protein
- A–E · 833 Ų buried · 12 hydrogen bonds · protein-protein
- B–F · 772 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 470 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 464 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 2 covalent (phosphorylation, covalent ligand).
Compared structures
- 1RQQ · Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of APS · the same entry in another collection · chain F against F, TM-score 1.00
- P06213 · AlphaFold monomer V2.0 prediction for insulin receptor (P06213) · a predicted model of the same protein · chain A against A, TM-score 0.93
- Q9Z200 · AlphaFold monomer V2.0 prediction for SH2B adapter protein 2 (Q9Z200) · a predicted model of the same protein · chain C against A, TM-score 0.79
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
- Every structure of UniProt Q9Z200
- Elsewhere: RCSB PDB 1RQQ · PDBe 1RQQ · UniProt P06213 · UniProt Q9Z200
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