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Crystal structure of an hfq-RNA complex
Analyse Crystal structure of an hfq-RNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KQ2
- Type
- protein + RNA
- Length
- 372 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-R(*AP*UP*UP*UP*UP*UP*G)-3'; Host factor for Q beta
- UniProt
- Q99UG9
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 4 distinct chains · 22% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| R | 5'-R(*AP*UP*UP*UP*UP*UP*G)-3' | rna | 7 | — | — |
| A, I | Host factor for Q beta | protein | 60 | 23% helix, 53% strand | Q99UG9 |
| B, K, M | Host factor for Q beta | protein | 61 | 18% helix, 49% strand | Q99UG9 |
| H | Host factor for Q beta | protein | 62 | 24% helix, 48% strand | Q99UG9 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 665 | 0.71 | 0.78 | 64 | empty |
| 2 | 79 | 0.41 | 0.78 | 13 | empty |
| 3 | 67 | 0.37 | 0.78 | 15 | empty |
| 4 | 60 | 0.35 | 0.78 | 13 | empty |
| 5 | 65 | 0.35 | 0.77 | 12 | empty |
Interfaces
12 interfaces between chains.
- B–M · 733 Ų buried · 12 hydrogen bonds · protein-protein
- K–M · 708 Ų buried · 10 hydrogen bonds · protein-protein
- H–I · 695 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 676 Ų buried · 10 hydrogen bonds · protein-protein
- A–H · 648 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1KQ2 · Crystal Structure of an Hfq-RNA Complex · the same entry in another collection · chain R against R, 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
- Every structure of UniProt Q99UG9
- Elsewhere: RCSB PDB 1KQ2 · PDBe 1KQ2 · UniProt Q99UG9
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