Research workbench
Crystal structure analysis of the BRD4
Analyse Crystal structure analysis of the BRD4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5Y94
- Type
- protein
- Length
- 126 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O60885
- Ligands
- 8QC, NA, NO3
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 126 | — | O60885 |
Ligands and binding sites
- 8QC · 5-bromanyl-2-methoxy-N-[3-methyl-6-(methylamino)-1,2-benzoxazol-5-yl]benzenesulfonamide · ligand · chains A
- NA · Sodium ion · metal · chains A
- NO3 · Nitrate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · chains A
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 O60885
- Elsewhere: RCSB PDB 5Y94 · PDBe 5Y94 · UniProt O60885
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