MolNFT v1 · #118038 · protein
Crystal structure of the human BRPF1 bromodomain in complex with SEED12
5EQ1 · Peregrin: “Crystal structure of the human BRPF1 bromodomain in complex with SEED12”. X-ray diffraction, 2 ligands (BEA, NO3), 1 pocket (best druggability 0.46). MolNFT v1 #118038 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5EQ1
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peregrin
- UniProt
- P55201
- Ligands
- BEA, NO3
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 66% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peregrin | protein | 112 | 66% helix, 0% strand | P55201 |
Ligands and binding sites
- BEA · 5-methyl-1,2,4-triazolo[3,4-b]benzothiazole · ligand · chains A
- NO3 · Nitrate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.46 | 0.82 | 17 | BEA |
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 P55201
- Elsewhere: RCSB PDB 5EQ1 · PDBe 5EQ1 · UniProt P55201
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.