MolNFT v1 · #156660 · protein
Human bfl-1 in complex with the designed peptide DF4
6MBC · BCL-2-related protein A1: “Human bfl-1 in complex with the designed peptide DF4”. X-ray diffraction, 1 ligand (ACE), 1 pocket (best druggability 0.32). MolNFT v1 #156660 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6MBC
- Type
- protein
- Length
- 175 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-related protein A1; DF4
- UniProt
- Q16548
- Ligands
- ACE
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BCL-2-related protein A1 | protein | 152 | 74% helix, 0% strand | Q16548 |
| B | DF4 | protein | 23 | 70% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains B
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 | 50 | 0.32 | 0.77 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 1186 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 Q16548
- Elsewhere: RCSB PDB 6MBC · PDBe 6MBC · UniProt Q16548
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