MolNFT v1 · #107775 · protein
Structure of melk in complex with inhibitors
4UMP · Maternal embryonic leucine zipper kinase: “Structure of melk in complex with inhibitors”. X-ray diffraction, 1 ligand (5QM), 14 pockets (best druggability 0.87). MolNFT v1 #107775 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4UMP
- Type
- protein
- Length
- 1,269 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maternal embryonic leucine zipper kinase
- EC
- 2.7.11.1, 2.7.10.2
- UniProt
- Q14680
- Ligands
- 5QM
- Pockets
- 14 · best druggability 0.87
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 313 | 43% helix, 15% strand | Q14680 |
| B | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 324 | 42% helix, 14% strand | Q14680 |
| C | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 311 | 41% helix, 15% strand | Q14680 |
| D | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 321 | 40% helix, 15% strand | Q14680 |
Ligands and binding sites
- 5QM · 3-(isoquinolin-7-yl)prop-2-yn-1-ol · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1117 | 0.87 | 0.88 | 120 | 5QM |
| 2 | 856 | 0.84 | 0.86 | 97 | 5QM |
| 3 | 625 | 0.84 | 0.88 | 76 | 5QM |
| 4 | 587 | 0.71 | 0.79 | 59 | empty |
| 5 | 364 | 0.70 | 0.82 | 42 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1424 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1266 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 561 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 294 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 19 Ų buried · 0 hydrogen bonds · protein-protein
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 4UMP · PDBe 4UMP · UniProt Q14680
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