Research workbench
An oligomeric domain-swapped beta-beta-alpha mini-protein
Analyse An oligomeric domain-swapped beta-beta-alpha mini-protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SN9
- Type
- protein
- Length
- 84 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tetrameric beta-beta-alpha mini-protein
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Tetrameric beta-beta-alpha mini-protein | protein | 21 | 57% helix, 10% strand | — |
Ligands and binding sites
- ACE · Acetyl group · ligand · 4 copies · chains A, B, C, D
- NH2 · Amino group · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
6 interfaces between chains.
- C–D · 502 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 494 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 420 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 392 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 74 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 d-amino, 4 covalent, 4 modified (D-amino acid, covalent ligand, nonstandard).
Compared structures
- 1SN9 · An Oligomeric Domain-Swapped Beta-Beta-Alpha Mini-Protein · 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 1SN9 · PDBe 1SN9
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