Research workbench
Lexa S119A mutant
Analyse Lexa S119A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JHH
- Type
- protein
- Length
- 316 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lexa repressor
- EC
- 3.4.21.88
- UniProt
- P0A7C2
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 16% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lexa repressor (EC 3.4.21.88) | protein | 197 | 23% helix, 31% strand | P0A7C2 |
| B | Lexa repressor (EC 3.4.21.88) | protein | 119 | 5% helix, 50% strand | P0A7C2 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.58 | 0.75 | 43 | empty |
| 2 | 110 | 0.45 | 0.78 | 18 | empty |
| 3 | 72 | 0.33 | 0.75 | 11 | empty |
| 4 | 66 | 0.32 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 705 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0A7C2
- Elsewhere: RCSB PDB 1JHH · PDBe 1JHH · UniProt P0A7C2
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