MolNFT v1 · #81703 · protein
Discovery of novel allosteric MEK inhibitors possessing classical and non-classical bidentate SER212 interactions.
3V01: “Discovery of novel allosteric MEK inhibitors possessing classical and non-classical bidentate SER212…”. X-ray diffraction. MolNFT v1 #81703 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3V01
- Type
- protein
- Length
- 289 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q02750
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 289 | — | Q02750 |
Compared structures
- 3V01 · Discovery of Novel Allosteric MEK Inhibitors Possessing Classical and Non-classical… · the same entry in another collection · chain A against A, TM-score 1.00
- Q02750 · AlphaFold monomer V2.0 prediction for dual specificity mitogen- activated protein kinase… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q02750
- Elsewhere: RCSB PDB 3V01 · PDBe 3V01 · UniProt Q02750
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