MolNFT v1 · #93302 · protein
Crystal structure of histidinol phosphate phosphatase (hisk) from lactococcus lactis subsp. lactis IL1403 complexed with zn, L- histidinol and phosphate
4GYF · Histidinol-phosphatase: “Crystal structure of histidinol phosphate phosphatase (hisk) from lactococcus lactis subsp. lactis IL1403…”. X-ray diffraction, 5 ligands (HSO, ZN, NA), 1 pocket (best druggability 0.43). MolNFT v1 #93302 on…
- PDB
- 4GYF
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidinol-phosphatase
- EC
- 3.1.3.15
- UniProt
- Q02150
- Ligands
- HSO, ZN, NA, CL, PO4
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphatase (EC 3.1.3.15) | protein | 263 | 41% helix, 18% strand | Q02150 |
Ligands and binding sites
- HSO · L-histidinol · ligand · 2 copies · chains A
- ZN · Zinc ion · metal · 4 copies · chains A
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · 6 copies · chains A
- PO4 · Phosphate ion · ion · chains A
- PEG · Di(hydroxyethyl)ether · additive · 3 copies · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.43 | 0.82 | 19 | PO4, HSO |
Compared structures
- 4GYF · Crystal structure of histidinol phosphate phosphatase (HISK) from Lactococcus lactis… · the same entry in another collection · chain A against A, TM-score 1.00
- Q02150 · AlphaFold monomer V2.0 prediction for histidinol-phosphatase (Q02150) · a predicted model of the same protein · 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 Q02150
- Elsewhere: RCSB PDB 4GYF · PDBe 4GYF · UniProt Q02150
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