MolNFT v1 · #6548 · protein
Crystal structure of L-histidinol phosphate aminotransferase complexed with L-histidinol
1FG3: “Crystal structure of L-histidinol phosphate aminotransferase complexed with L-histidinol”. X-ray diffraction, 2 ligands (PLP, HSA), 1 pocket (best druggability 0.64). MolNFT v1 #6548 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1FG3
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidinol phosphate aminotransferase
- EC
- 2.6.1.9
- UniProt
- P06986
- Ligands
- PLP, HSA
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol phosphate aminotransferase (EC 2.6.1.9) | protein | 354 | 40% helix, 16% strand | P06986 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
- HSA · Phosphoric acid mono-[2-amino-3-(3H-imidazol-4-yl)-propyl]ester · ligand · chains A
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 | 396 | 0.64 | 0.78 | 52 | PLP, HSA |
Modifications
Observed in the structure: 3 modified, 1 cofactor (engineered, pyridoxal phosphate Schiff base).
Compared structures
- 1FG3 · Crystal structure of L-histidinol phosphate aminotransferase complexed with L-histidinol · the same entry in another collection · chain A against A, TM-score 1.00
- P06986 · AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (P06986) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P06986
- Elsewhere: RCSB PDB 1FG3 · PDBe 1FG3 · UniProt P06986
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