Research workbench
Biochemical, cellular and structural characterization of novel ERK3 inhibitors
Analyse Biochemical, cellular and structural characterization of novel ERK3 inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YLL
- Type
- protein
- Length
- 538 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q16659
- Ligands
- OYB
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 293 | — | Q16659 |
| B | — | protein | 245 | — | Q16659 |
Ligands and binding sites
- OYB · ~{N}4-[3-(4-methoxyphenyl)-[1,2,3]triazolo[4,5-d]pyrimidin-5-yl]cyclohexane-1,4-diamine · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6YLL · Biochemical, Cellular and Structural Characterization of Novel ERK3 Inhibitors · the same entry in another collection · chain A against A, TM-score 1.00
- Q16659 · AlphaFold monomer V2.0 prediction for mitogen-activated protein kinase 6 (Q16659) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 Q16659
- Elsewhere: RCSB PDB 6YLL · PDBe 6YLL · UniProt Q16659
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