MolNFT v1 · #183617 · protein
Crystal structure of the tg and EGF-like domains of ALK
7NX4 · ALK tyrosine kinase receptor: “Crystal structure of the tg and EGF-like domains of ALK”. X-ray diffraction, 3 ligands (NAG, NI, ZN), 2 pockets (best druggability 0.55). MolNFT v1 #183617 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7NX4
- Type
- protein
- Length
- 348 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
- NAG, NI, ZN
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALK tyrosine kinase receptor (EC 2.7.10.1) | protein | 348 | 8% helix, 20% strand | Q9UM73 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- NI · Nickel (II) ion · metal · 2 copies · chains A
- ZN · Zinc ion · metal · 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 | 185 | 0.55 | 0.79 | 33 | empty |
| 2 | 122 | 0.48 | 0.79 | 25 | NI |
Modifications
Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).
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 7NX4 · PDBe 7NX4 · UniProt Q9UM73
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