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Macrocyclization of an all-D linear peptide improves target affinity and imparts cellular activity: A novel stapled alpha-helical peptide modality
Analyse Macrocyclization of an all-D linear peptide improves target affinity and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KZU
- Type
- protein
- Length
- 97 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.79
- Source
- Homo sapiens; SYNTHETIC CONSTRUCT
- Molecule
- E3 ubiquitin-protein ligase Mdm2; 2JN-dal-E03-dty-2JN-dsg-tdf-dgl-MK8-dle-dle-2JN
- EC
- 2.3.2.27
- UniProt
- Q00987
Structure
x-ray diffraction · resolution 1.79 · 2 distinct chains · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase Mdm2 (EC 2.3.2.27) | protein | 85 | 46% helix, 22% strand | Q00987 |
| B | 2JN-dal-E03-dty-2JN-dsg-tdf-dgl-MK8-dle-dle-2JN | protein | 12 | 58% helix, 0% strand | — |
Interfaces
1 interface between chains.
- A–B · 681 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 d-amino, 6 modified (D-amino acid, nonstandard).
Compared structures
- 6KZU · Macrocyclization of an all-D linear peptide improves target affinity and imparts cellular… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q00987
- Elsewhere: RCSB PDB 6KZU · PDBe 6KZU · UniProt Q00987
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