Research workbench
Melk in complex with nvs-MELK8A
Analyse Melk in complex with nvs-MELK8A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IH9
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maternal embryonic leucine zipper kinase
- EC
- 2.7.11.1
- UniProt
- Q14680
- Ligands
- 6BF
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maternal embryonic leucine zipper kinase (EC 2.7.11.1) | protein | 308 | 44% helix, 15% strand | Q14680 |
Ligands and binding sites
- 6BF · 1-methyl-4-[4-(4-{3-[(piperidin-4-yl)methoxy]pyridin-4-yl}-1H-pyrazol-1-yl)phenyl]piperazine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.66 | 0.81 | 34 | 6BF |
| 2 | 249 | 0.60 | 0.80 | 30 | empty |
| 3 | 84 | 0.36 | 0.76 | 12 | empty |
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 Q14680
- Elsewhere: RCSB PDB 5IH9 · PDBe 5IH9 · UniProt Q14680
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