Research workbench
Crystal structure of ALK in complex with FAB324
Analyse Crystal structure of ALK in complex with FAB324 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NX3
- Type
- protein
- Length
- 1,438 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALK tyrosine kinase receptor; FAB324 heavychain; FAB324 light chain
- EC
- 2.7.10.1
- UniProt
- Q9UM73
- Ligands
- NAG
- Pockets
- 17 · best druggability 0.79
Structure
x-ray diffraction · 5 distinct chains · 9% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALK tyrosine kinase receptor (EC 2.7.10.1) | protein | 292 | 9% helix, 24% strand | Q9UM73 |
| B | FAB324 heavychain | protein | 209 | 9% helix, 54% strand | — |
| C, D | FAB324 light chain | protein | 216 | 6% helix, 51% strand | — |
| E | FAB324 heavychain | protein | 212 | 8% helix, 54% strand | — |
| F | ALK tyrosine kinase receptor (EC 2.7.10.1) | protein | 293 | 10% helix, 25% strand | Q9UM73 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, C, F, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1058 | 0.79 | 0.81 | 140 | empty |
| 2 | 415 | 0.64 | 0.78 | 60 | empty |
| 3 | 325 | 0.64 | 0.80 | 53 | empty |
| 4 | 182 | 0.47 | 0.75 | 35 | empty |
| 5 | 202 | 0.46 | 0.74 | 28 | empty |
Interfaces
9 interfaces between chains.
- D–E · 1858 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 1753 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 942 Ų buried · 15 hydrogen bonds · protein-protein
- D–F · 922 Ų buried · 15 hydrogen bonds · protein-protein
- A–E · 745 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 7 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 7NX3 · PDBe 7NX3 · UniProt Q9UM73
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