MolNFT v1 · #110080 · protein
Crystal structure of the activated insulin receptor tyrosine kinase dimer
4XLV: “Crystal structure of the activated insulin receptor tyrosine kinase dimer”. X-ray diffraction, 2 ligands (ACP, MG), 5 pockets (best druggability 0.64). MolNFT v1 #110080 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4XLV
- Type
- protein
- Length
- 310 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Insulin receptor
- EC
- 2.7.10.1
- UniProt
- P06213
- Ligands
- ACP, MG
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Insulin receptor (EC 2.7.10.1) | protein | 310 | 37% helix, 18% strand | P06213 |
Ligands and binding sites
- ACP · Phosphomethylphosphonic acid adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 396 | 0.64 | 0.78 | 50 | ACP, MG |
| 2 | 82 | 0.44 | 0.80 | 21 | empty |
| 3 | 65 | 0.30 | 0.74 | 17 | empty |
| 4 | 65 | 0.30 | 0.74 | 16 | empty |
| 5 | 61 | 0.30 | 0.74 | 13 | empty |
Modifications
Observed in the structure: 3 modified (phosphorylation).
Compared structures
- 4XLV · Crystal structure of the activated insulin receptor tyrosine kinase dimer · the same entry in another collection · chain A against A, 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 0.90
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 4XLV · PDBe 4XLV · UniProt P06213
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