MolNFT v1 · #115276 · protein
Dlk in complex with inhibitor 2-((1-cyclopentyl-5-(1-(oxetan-3-yl) piperidin-4-yl)-1H-pyrazol-3-YL)AMINO)ISONICOTINONITRILE
5CEQ · Mitogen-activated protein kinase kinase kinase 12: “Dlk in complex with inhibitor 2-((1-cyclopentyl-5-(1-(oxetan-3-yl)…”. X-ray diffraction, 1 ligand (50F), 2 pockets (best druggability 0.58). MolNFT v1 #115276 on GenesisL1: 3D…
- PDB
- 5CEQ
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitogen-activated protein kinase kinase kinase 12
- EC
- 2.7.11.25
- UniProt
- Q12852
- Ligands
- 50F
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitogen-activated protein kinase kinase kinase 12 (EC 2.7.11.25) | protein | 269 | 45% helix, 16% strand | Q12852 |
Ligands and binding sites
- 50F · 2-[[1-cyclopentyl-5-[1-(oxetan-3-yl)piperidin-4-yl]pyrazol-3-yl]amino]pyridine-4-carbonitrile · ligand · chains A
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 | 124 | 0.58 | 0.84 | 23 | 50F |
| 2 | 62 | 0.38 | 0.79 | 17 | empty |
Compared structures
- 5CEQ · DLK in complex with inhibitor 2-((1-cyclopentyl-5-(1-(oxetan-3-yl)piperidin-4-yl)-1H-pyraz… · the same entry in another collection · chain A against A, TM-score 1.00
- Q12852 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase kinase kinase 12… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q12852
- Elsewhere: RCSB PDB 5CEQ · PDBe 5CEQ · UniProt Q12852
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