MolNFT v1 · #135086 · protein
Selectivity switch between fak and PYK2: macrocyclization of fak inhibitors improves PYK2 potency
5TOB: “Selectivity switch between fak and PYK2: macrocyclization of fak inhibitors improves PYK2 potency”. X-ray diffraction, 1 ligand (YAM). MolNFT v1 #135086 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5TOB
- Type
- protein
- Length
- 245 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q14289
- Ligands
- YAM
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 245 | — | Q14289 |
Ligands and binding sites
- YAM · N-methyl-N-{3-[({2-[(2-oxo-2,3-dihydro-1H-indol-5-yl) amino]-5-(trifluoromethyl)pyrimidin-4-yl}amino) methyl]pyridin-2-yl}methanesulfonamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5TOB · Selectivity switch between FAK and Pyk2: Macrocyclization of FAK inhibitors improves Pyk2… · the same entry in another collection · chain A against A, TM-score 1.00
- Q14289 · AlphaFold monomer V2.0 prediction for protein-tyrosine kinase 2-beta (Q14289) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q14289
- Elsewhere: RCSB PDB 5TOB · PDBe 5TOB · UniProt Q14289
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