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Crystal structure of domain-swapped dimer of H5_FOLD-0 elsa; de novo designed protein with an asymmetric all-alpha topology
Analyse Crystal structure of domain-swapped dimer of H5_FOLD-0 elsa; de novo designed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DNS
- Type
- protein
- Length
- 178 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- De novo designed protein
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | De novo designed protein | protein | 90 | 82% helix, 0% strand | — |
| B | De novo designed protein | protein | 88 | 82% helix, 0% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · chains A, B
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 | 78 | 0.38 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1603 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 7DNS · Crystal structure of domain-swapped dimer of H5_Fold-0 Elsa; de novo designed 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 7DNS · PDBe 7DNS
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