MolNFT v1 · #159443 · protein
Phosphorylated ERK2 with sch-CPD336
6OPI: “Phosphorylated ERK2 with sch-CPD336”. X-ray diffraction, 1 ligand (N0V). MolNFT v1 #159443 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6OPI
- Type
- protein
- Length
- 326 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P28482
- Ligands
- N0V
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 326 | — | P28482 |
Ligands and binding sites
- N0V · (3R)-N-[3-(2-cyclopropylpyridin-4-yl)-1H-indazol-5-yl]-3-(methoxymethyl)-1-(2-oxo-2-{4-[4-(pyrimidin-2-yl) phenyl]-3,6-dihydropyridin-1(2H)-yl}ethyl)pyrrolidine-3-carboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OPI · phosphorylated ERK2 with SCH-CPD336 · 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 6OPI · PDBe 6OPI · UniProt P28482
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