MolNFT v1 · #64094 · protein
The crystal structure of the histidinol-phosphate aminotransferase from clostridium acetobutylicum
3FTB: “The crystal structure of the histidinol-phosphate aminotransferase from clostridium acetobutylicum”. X-ray diffraction, 1 ligand (PO4), 19 pockets (best druggability 0.67). MolNFT v1 #64094 on GenesisL1: 3D structure, binding sites…
- PDB
- 3FTB
- Type
- protein
- Length
- 1,335 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidinol-phosphate aminotransferase
- UniProt
- Q97JB7
- Ligands
- PO4
- Pockets
- 19 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | Histidinol-phosphate aminotransferase | protein | 334 | 41% helix, 19% strand | Q97JB7 |
| D | Histidinol-phosphate aminotransferase | protein | 333 | 40% helix, 18% strand | Q97JB7 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 10 copies · chains A, B, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 227 | 0.67 | 0.85 | 27 | empty |
| 2 | 228 | 0.66 | 0.84 | 24 | empty |
| 3 | 394 | 0.65 | 0.79 | 57 | PO4 |
| 4 | 377 | 0.65 | 0.79 | 53 | PO4 |
| 5 | 254 | 0.63 | 0.81 | 42 | PO4 |
Interfaces
3 interfaces between chains.
- A–B · 1336 Ų buried · 22 hydrogen bonds · protein-protein
- D–E · 1327 Ų buried · 19 hydrogen bonds · protein-protein
- B–E · 234 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3FTB · The crystal structure of the histidinol-phosphate aminotransferase from Clostridium… · the same entry in another collection · chain A against A, 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 Q97JB7
- Elsewhere: RCSB PDB 3FTB · PDBe 3FTB · UniProt Q97JB7
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