Research workbench
Designed protein KE59 R5_11/5F
Analyse Designed protein KE59 R5_11/5F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UY8
- Type
- protein
- Length
- 493 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kemp eliminase KE59 R5_11/5F
- EC
- 4.-.-.-
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kemp eliminase KE59 R5_11/5F (EC 4.-.-.-) | protein | 246 | 39% helix, 17% strand | — |
| B | Kemp eliminase KE59 R5_11/5F (EC 4.-.-.-) | protein | 247 | 40% helix, 17% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 198 | 0.75 | 0.90 | 36 | SO4 |
| 2 | 193 | 0.73 | 0.89 | 32 | SO4 |
| 3 | 326 | 0.67 | 0.81 | 44 | empty |
Interfaces
1 interface between chains.
- A–B · 751 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 3UY8 · Designed protein KE59 R5_11/5F · 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 3UY8 · PDBe 3UY8
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