MolNFT v1 · #106886 · protein
Crystal structure of human ALK with a covalent modification
4TT7 · ALK tyrosine kinase receptor: “Crystal structure of human ALK with a covalent modification”. X-ray diffraction, 1 ligand (COM), 2 pockets (best druggability 0.56). MolNFT v1 #106886 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4TT7
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALK tyrosine kinase receptor
- EC
- 2.7.10.1
- UniProt
- Q9UM73
- Ligands
- COM
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALK tyrosine kinase receptor (EC 2.7.10.1) | protein | 291 | 44% helix, 16% strand | Q9UM73 |
Ligands and binding sites
- COM · 1-thioethanesulfonic acid · ligand · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.56 | 0.79 | 27 | empty |
| 2 | 160 | 0.44 | 0.75 | 28 | COM |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
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 Q9UM73
- Elsewhere: RCSB PDB 4TT7 · PDBe 4TT7 · UniProt Q9UM73
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