MolNFT v1 · #145300 · protein
Crystal structure of MNK2-D228G in complex with inhibitor
6CJW · MAP kinase-interacting SERINE/THREONINE-protein kinase 2: “Crystal structure of MNK2-D228G in complex with inhibitor”. X-ray diffraction, 2 ligands (FYV, ZN), 2 pockets (best druggability 0.68). MolNFT v1 #145300 on GenesisL1: 3D…
- PDB
- 6CJW
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MAP kinase-interacting SERINE/THREONINE-protein kinase 2
- EC
- 2.7.11.1
- UniProt
- Q9HBH9
- Ligands
- FYV, ZN
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MAP kinase-interacting SERINE/THREONINE-protein kinase 2 (EC 2.7.11.1) | protein | 270 | 40% helix, 14% strand | Q9HBH9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.68 | 0.81 | 41 | FYV |
| 2 | 122 | 0.40 | 0.74 | 21 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6CJW · Crystal Structure of Mnk2-D228G in Complex With Inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HBH9 · AlphaFold monomer V2.0 prediction for MAP kinase-interacting SERINE/THREONINE-protein… · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q9HBH9
- Elsewhere: RCSB PDB 6CJW · PDBe 6CJW · UniProt Q9HBH9
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