Research workbench
Structure of the periplasmic domain phoq double mutant (W104C-A128C)
Analyse Structure of the periplasmic domain phoq double mutant (W104C-A128C) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UEY
- Type
- protein
- Length
- 420 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phoq periplasmic domain double mutant
- UniProt
- P0DM80
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phoq periplasmic domain double mutant | protein | 140 | 34% helix, 33% strand | P0DM80 |
| B, C | Phoq periplasmic domain double mutant | protein | 140 | 31% helix, 33% strand | P0DM80 |
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 | 1110 | 0.77 | 0.79 | 73 | empty |
| 2 | 103 | 0.46 | 0.79 | 16 | empty |
| 3 | 61 | 0.34 | 0.77 | 17 | empty |
| 4 | 58 | 0.33 | 0.77 | 15 | empty |
Interfaces
3 interfaces between chains.
- A–B · 522 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 514 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 501 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4UEY · Structure of the periplasmic domain PhoQ double mutant (W104C-A128C) · the same entry in another collection · chain A against A, TM-score 1.00
- P0DM80 · AlphaFold monomer V2.0 prediction for virulence sensor histidine kinase phoq (P0DM80) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 P0DM80
- Elsewhere: RCSB PDB 4UEY · PDBe 4UEY · UniProt P0DM80
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