MolNFT v1 · #88689 · protein
Structure of melk in complex with inhibitors
4D2T · Maternal embryonic leucine zipper kinase: “Structure of melk in complex with inhibitors”. X-ray diffraction, 1 ligand (3I7), 17 pockets (best druggability 0.83). MolNFT v1 #88689 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 4D2T
- Type
- protein
- Length
- 1,271 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
- 3I7
- Pockets
- 17 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 39% helix, 13% 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 | 316 | 39% helix, 12% strand | Q14680 |
| B | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 323 | 39% helix, 14% strand | Q14680 |
| C | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 313 | 39% helix, 13% strand | Q14680 |
| D | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 319 | 38% helix, 13% strand | Q14680 |
Ligands and binding sites
- 3I7 · 3-[2-(phenylcarbamoyl)-5-(1H-pyrazol-4-yl)phenoxy]propan-1-aminium · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 792 | 0.83 | 0.86 | 77 | 3I7 |
| 2 | 987 | 0.82 | 0.83 | 86 | 3I7 |
| 3 | 940 | 0.80 | 0.82 | 79 | 3I7 |
| 4 | 1157 | 0.78 | 0.80 | 82 | 3I7 |
| 5 | 191 | 0.66 | 0.85 | 26 | empty |
Interfaces
4 interfaces between chains.
- B–C · 979 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 810 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 563 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 386 Ų buried · 3 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 4D2T · PDBe 4D2T · UniProt Q14680
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