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The crystal structure of hfq from caulobacter crescentus
Analyse The crystal structure of hfq from caulobacter crescentus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GWK
- Type
- protein
- Length
- 1,651 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-binding protein hfq
- UniProt
- Q9A7H8
- Pockets
- 11 · best druggability 0.76
Structure
x-ray diffraction · 15 distinct chains · 21% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, I, W | RNA-binding protein hfq | protein | 63 | 22% helix, 51% strand | Q9A7H8 |
| B, D, J, P, V | RNA-binding protein hfq | protein | 77 | 18% helix, 42% strand | Q9A7H8 |
| C | RNA-binding protein hfq | protein | 69 | 20% helix, 46% strand | Q9A7H8 |
| E | RNA-binding protein hfq | protein | 67 | 16% helix, 48% strand | Q9A7H8 |
| F, O | RNA-binding protein hfq | protein | 68 | 21% helix, 44% strand | Q9A7H8 |
| G | RNA-binding protein hfq | protein | 64 | 23% helix, 45% strand | Q9A7H8 |
| H, N | RNA-binding protein hfq | protein | 76 | 20% helix, 37% strand | Q9A7H8 |
| K | RNA-binding protein hfq | protein | 60 | 25% helix, 52% strand | Q9A7H8 |
| L | RNA-binding protein hfq | protein | 70 | 21% helix, 44% strand | Q9A7H8 |
| M | RNA-binding protein hfq | protein | 66 | 21% helix, 48% strand | Q9A7H8 |
| Q | RNA-binding protein hfq | protein | 61 | 23% helix, 52% strand | Q9A7H8 |
| R | RNA-binding protein hfq | protein | 71 | 20% helix, 46% strand | Q9A7H8 |
| S, U | RNA-binding protein hfq | protein | 62 | 23% helix, 52% strand | Q9A7H8 |
| T | RNA-binding protein hfq | protein | 70 | 17% helix, 37% strand | Q9A7H8 |
| X | RNA-binding protein hfq | protein | 67 | 21% helix, 48% strand | Q9A7H8 |
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 674 | 0.76 | 0.81 | 56 | empty |
| 2 | 634 | 0.75 | 0.81 | 78 | empty |
| 3 | 654 | 0.74 | 0.80 | 72 | empty |
| 4 | 868 | 0.71 | 0.76 | 66 | empty |
| 5 | 928 | 0.71 | 0.75 | 66 | empty |
Interfaces
37 interfaces between chains.
- N–R · 1149 Ų buried · 18 hydrogen bonds · protein-protein
- H–L · 1138 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1137 Ų buried · 14 hydrogen bonds · protein-protein
- T–X · 1121 Ų buried · 14 hydrogen bonds · protein-protein
- O–P · 1117 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 6GWK · The crystal structure of Hfq from Caulobacter crescentus · the same entry in another collection · chain G against G, 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 Q9A7H8
- Elsewhere: RCSB PDB 6GWK · PDBe 6GWK · UniProt Q9A7H8
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