Research workbench
Crystal structure of darpin-darpin rigid fusion, variant DDD_D12_15_D12_15_D12
Analyse Crystal structure of darpin-darpin rigid fusion, variant DDD_D12_15_D12_15_D12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LE2
- Type
- protein
- Length
- 958 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DDD_D12_15_D12_15_D12
- Ligands
- SCN
- Pockets
- 3 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | DDD_D12_15_D12_15_D12 | protein | 479 | 57% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.30 | 0.74 | 19 | empty |
| 2 | 56 | 0.29 | 0.74 | 15 | empty |
| 3 | 66 | 0.28 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 66 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5LE2 · Crystal structure of DARPin-DARPin rigid fusion, variant DDD_D12_15_D12_15_D12 · 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 5LE2 · PDBe 5LE2
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