MolNFT v1 · #156659 · protein
Human bfl-1 in complex with the designed peptide DF1
6MBB · BCL-2-related protein A1: “Human bfl-1 in complex with the designed peptide DF1”. X-ray diffraction, 2 ligands (ACE, NH2), 1 pocket (best druggability 0.32). MolNFT v1 #156659 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6MBB
- Type
- protein
- Length
- 174 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-related protein A1; DF1
- UniProt
- Q16548
- Ligands
- ACE, NH2
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 76% 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 | DF1 | protein | 22 | 86% helix, 0% strand | — |
Ligands and binding sites
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 | 57 | 0.32 | 0.77 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 963 Ų buried · 8 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 6MBB · PDBe 6MBB · UniProt Q16548
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