MolNFT v2 · #172867 · protein
Human Brd2(BD2) L383V mutant in complex with ET-JQ1-OMe
6YTM: “Human Brd2(BD2) L383V mutant in complex with ET-JQ1-OMe”. X-ray diffraction at 1.56, 2 ligands (PMW, PXN). MolNFT v2 #172867 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YTM
- Type
- protein
- Length
- 218 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.56
- Source
- Homo sapiens
- UniProt
- P25440
- Ligands
- PMW, PXN
Structure
x-ray diffraction · resolution 1.56 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 110 | — | P25440 |
| B | — | protein | 108 | — | P25440 |
Ligands and binding sites
- PMW · Methyl (R)-2-((S)-4-(4-chlorophenyl)-2,3,9-trimethyl-6H-thieno[3,2-f][1,2,4]triazolo[4,3-a][1,4]diazepin-6-yl)butanoate · ligand · 2 copies · chains A, B
- PXN · (2S)-1-[3-{[(2R)-2-hydroxypropyl]oxy}-2,2-bis({[(2R)-2-hydroxypropyl]oxy}methyl)propoxy]propan-2-ol · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 P25440
- Elsewhere: RCSB PDB 6YTM · PDBe 6YTM · UniProt P25440
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