MolNFT v1 · #147128 · protein
Human bfl-1 in complex with the bfl-1-specific designed peptide SRT.F10
6E3J · BCL-2-related protein A1: “Human bfl-1 in complex with the bfl-1-specific designed peptide SRT.F10”. X-ray diffraction, 3 ligands (ACE, NH2, SO4), 1 pocket (best druggability 0.32). MolNFT v1 #147128 on GenesisL1: 3D structure…
- PDB
- 6E3J
- Type
- protein
- Length
- 173 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BCL-2-related protein A1; Peptide SRT.F10
- UniProt
- Q16548
- Ligands
- ACE, NH2, SO4
- 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 | Peptide SRT.F10 | protein | 21 | 90% helix, 0% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · chains B
- NH2 · Amino group · ion · chains A, B
- SO4 · Sulfate 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 | 59 | 0.32 | 0.76 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 946 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6E3J · Human Bfl-1 in complex with the Bfl-1-specific designed peptide srt.F10 · the same entry in another collection · chain A against A, TM-score 1.00
- Q16548 · AlphaFold monomer V2.0 prediction for BCL-2-related protein A1 (Q16548) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 6E3J · PDBe 6E3J · UniProt Q16548
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