Research workbench
Structure of melk in complex with inhibitors
Analyse Structure of melk in complex with inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4D2V
- 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
- 45R
- Pockets
- 17 · best druggability 0.85
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 | 313 | 40% helix, 13% strand | Q14680 |
| B | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 322 | 39% helix, 12% strand | Q14680 |
| C | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 316 | 41% helix, 13% strand | Q14680 |
| D | Maternal embryonic leucine zipper kinase (EC 2.7.11.1, 2.7.10.2) | protein | 318 | 37% helix, 14% strand | Q14680 |
Ligands and binding sites
- 45R · 7-{[2-methoxy-4-(1H-pyrazol-4-yl)benzoyl]amino}-2,3,4, 5-tetrahydro-1H-3-benzazepinium · 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, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 711 | 0.85 | 0.88 | 80 | 45R |
| 2 | 665 | 0.84 | 0.88 | 76 | 45R |
| 3 | 905 | 0.83 | 0.85 | 96 | 45R |
| 4 | 415 | 0.82 | 0.90 | 54 | 45R |
| 5 | 142 | 0.67 | 0.88 | 22 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1300 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 1222 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 513 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 365 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 42 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 4D2V · PDBe 4D2V · UniProt Q14680
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