MolNFT v1 · #40069 · protein
Crystal structure of immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase musk
2IEP · Muscle-specific kinase receptor: “Crystal structure of immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase musk”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.41). MolNFT v1 #40069 on GenesisL1…
- PDB
- 2IEP
- Type
- protein
- Length
- 374 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Muscle-specific kinase receptor
- EC
- 2.7.10.1
- UniProt
- Q62838
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Muscle-specific kinase receptor (EC 2.7.10.1) | protein | 187 | 5% helix, 56% strand | Q62838 |
| B | Muscle-specific kinase receptor (EC 2.7.10.1) | protein | 187 | 3% helix, 56% strand | Q62838 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.41 | 0.81 | 16 | empty |
| 2 | 52 | 0.28 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 682 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 2IEP · Crystal structure of immunoglobulin-like domains 1 and 2 of the receptor tyrosine kinase… · the same entry in another collection · chain A against A, TM-score 1.00
- Q62838 · AlphaFold monomer V2.0 prediction for muscle, skeletal receptor tyrosine protein kinase… · a predicted model of the same protein · chain B against A, TM-score 0.97
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 Q62838
- Elsewhere: RCSB PDB 2IEP · PDBe 2IEP · UniProt Q62838
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