MolNFT v1 · #96000 · protein
Hfq from pseudomonas aeruginosa crystallized in GTP presence
4J6Y · Protein hfq: “Hfq from pseudomonas aeruginosa crystallized in GTP presence”. X-ray diffraction, 1 ligand (CD), 1 pocket (best druggability 0.70). MolNFT v1 #96000 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4J6Y
- Type
- protein
- Length
- 399 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein hfq
- UniProt
- Q9HUM0
- Ligands
- CD
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 3 distinct chains · 20% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Protein hfq | protein | 66 | 20% helix, 45% strand | Q9HUM0 |
| B | Protein hfq | protein | 66 | 20% helix, 44% strand | Q9HUM0 |
| C, E, F | Protein hfq | protein | 67 | 19% helix, 43% strand | Q9HUM0 |
Ligands and binding sites
- CD · Cadmium ion · metal · 12 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 908 | 0.70 | 0.75 | 59 | CD |
Interfaces
6 interfaces between chains.
- C–D · 834 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 802 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 795 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 794 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 786 Ų buried · 14 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 4J6Y · PDBe 4J6Y · UniProt Q9HUM0
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