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Crystal structure of a thermotoga maritima hfq homolog
Analyse Crystal structure of a thermotoga maritima hfq homolog in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y91
- Type
- protein + RNA
- Length
- 809 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-binding protein hfq; RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3')
- UniProt
- Q9WYZ6
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · 5 distinct chains · 20% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-binding protein hfq | protein | 66 | 21% helix, 50% strand | Q9WYZ6 |
| B, D, E, G, H, J, K, L | RNA-binding protein hfq | protein | 66 | 21% helix, 48% strand | Q9WYZ6 |
| C, I | RNA-binding protein hfq | protein | 65 | 22% helix, 51% strand | Q9WYZ6 |
| F | RNA-binding protein hfq | protein | 73 | 18% helix, 44% strand | Q9WYZ6 |
| N, O | RNA (5'-R(P*UP*UP*UP*UP*UP*U)-3') | rna | 6 | — | — |
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 548 | 0.77 | 0.84 | 36 | empty |
| 2 | 462 | 0.77 | 0.85 | 30 | empty |
| 3 | 256 | 0.61 | 0.80 | 31 | empty |
| 4 | 51 | 0.35 | 0.79 | 20 | empty |
| 5 | 75 | 0.34 | 0.75 | 13 | empty |
Interfaces
27 interfaces between chains.
- K–L · 872 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 864 Ų buried · 16 hydrogen bonds · protein-protein
- G–L · 856 Ų buried · 14 hydrogen bonds · protein-protein
- E–F · 849 Ų buried · 11 hydrogen bonds · protein-protein
- J–K · 842 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4Y91 · Crystal Structure of a Thermotoga maritima Hfq homolog · the same entry in another collection · chain O against O, 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 Q9WYZ6
- Elsewhere: RCSB PDB 4Y91 · PDBe 4Y91 · UniProt Q9WYZ6
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