MolNFT v1 · #183465 · protein
Discovery of ASTX029, a clinical candidate which modulates the phosphorylation and catalytic activity of ERK1/2
7NQW: “Discovery of ASTX029, a clinical candidate which modulates the phosphorylation and catalytic activity of…”. X-ray diffraction, 2 ligands (UNW, SO4). MolNFT v1 #183465 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7NQW
- Type
- protein
- Length
- 346 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P28482
- Ligands
- UNW, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 346 | — | P28482 |
Ligands and binding sites
- UNW · 6-[5-chloranyl-2-(oxan-4-ylamino)pyrimidin-4-yl]-2-[2-oxidanylidene-2-(1,3,4,5-tetrahydro-2-benzazepin-2-yl)ethyl]-3~{H}-isoindol-1-one · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- DMS · Dimethyl sulfoxide · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NQW · Discovery of ASTX029, a clinical candidate which modulates the phosphorylation and… · the same entry in another collection · chain A against A, TM-score 1.00
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 P28482
- Elsewhere: RCSB PDB 7NQW · PDBe 7NQW · UniProt P28482
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