Research workbench
Crystal structure of the mertk kinase domain in complex with inhibitor MIPS15692
Analyse Crystal structure of the mertk kinase domain in complex with inhibitor MIPS15692 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7M5Z
- Type
- protein
- Length
- 527 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tyrosine-protein kinase mer
- EC
- 2.7.10.1
- UniProt
- Q12866
- Ligands
- YR7
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tyrosine-protein kinase mer (EC 2.7.10.1) | protein | 263 | 41% helix, 21% strand | Q12866 |
| B | Tyrosine-protein kinase mer (EC 2.7.10.1) | protein | 264 | 38% helix, 18% strand | Q12866 |
Ligands and binding sites
- YR7 · 2-(butylamino)-N-[1-(3-fluoropropyl)piperidin-4-yl]-4-{[(1r,4r)-4-hydroxycyclohexyl]amino}pyrimidine-5-carboxamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1104 | 0.76 | 0.78 | 103 | YR7 |
| 2 | 311 | 0.62 | 0.79 | 40 | empty |
| 3 | 83 | 0.41 | 0.78 | 22 | empty |
| 4 | 73 | 0.29 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1050 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7M5Z · Crystal Structure of the MerTK Kinase Domain in Complex with Inhibitor MIPS15692 · the same entry in another collection · chain A against A, 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 Q12866
- Elsewhere: RCSB PDB 7M5Z · PDBe 7M5Z · UniProt Q12866
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.