MolNFT v2 · #220599 · protein
De novo design of high-affinity protein binders to bioactive helical peptides
8T5E · Bim_fulldiff: “De novo design of high-affinity protein binders to bioactive helical peptides”. X-ray diffraction at 3. MolNFT v2 #220599 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8T5E
- Type
- protein
- Length
- 152 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3
- Source
- synthetic construct; SYNTHETIC CONSTRUCT
- Molecule
- Bim_fulldiff; Bcl-2-like protein 11
- UniProt
- O43521
Structure
x-ray diffraction · resolution 3 · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bim_fulldiff | protein | 130 | 82% helix, 0% strand | — |
| B | Bcl-2-like protein 11 | protein | 22 | 73% helix, 0% strand | O43521 |
Interfaces
1 interface between chains.
- A–B · 1129 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- O43521 · AlphaFold monomer V2.0 prediction for BCL-2-like protein 11 (O43521) · a predicted model of the same protein · chain B against A, TM-score 0.60
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 O43521
- Elsewhere: RCSB PDB 8T5E · PDBe 8T5E · UniProt O43521
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