Research workbench
Hfq protein from pseudomonas aeruginosa. high-salt crystals
Analyse Hfq protein from pseudomonas aeruginosa. high-salt crystals in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U1T
- Type
- protein
- Length
- 398 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hfq protein
- UniProt
- Q9HUM0
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 20% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Hfq protein | protein | 66 | 20% helix, 45% strand | Q9HUM0 |
| B, F | Hfq protein | protein | 66 | 20% helix, 44% strand | Q9HUM0 |
| C | Hfq protein | protein | 65 | 20% helix, 45% strand | Q9HUM0 |
| E | Hfq protein | protein | 69 | 19% helix, 43% strand | Q9HUM0 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 917 | 0.71 | 0.75 | 67 | empty |
Interfaces
6 interfaces between chains.
- D–E · 807 Ų buried · 11 hydrogen bonds · protein-protein
- A–F · 784 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 777 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 725 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 720 Ų buried · 11 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 Q9HUM0
- Elsewhere: RCSB PDB 1U1T · PDBe 1U1T · UniProt Q9HUM0
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