Research workbench
The de novo designed hybrid ALPHA/BETA-miniprotein (with se- methionine)
Analyse The de novo designed hybrid ALPHA/BETA-miniprotein (with se- methionine) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ARS
- Type
- protein
- Length
- 62 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALPHA/BETA-peptide
- Ligands
- MG
Structure
x-ray diffraction · 2 distinct chains · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ALPHA/BETA-peptide | protein | 35 | 69% helix, 0% strand | — |
| B | ALPHA/BETA-peptide | protein | 27 | 78% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 678 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (nonstandard, engineered).
Compared structures
- 7ARS · The de novo designed hybrid alpha/beta-miniprotein (with Se-Methionine) · 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
- Elsewhere: RCSB PDB 7ARS · PDBe 7ARS
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