Research workbench
Histidinol phosphate phosphatase complexed with phosphate
Analyse Histidinol phosphate phosphatase complexed with phosphate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YZ5
- Type
- protein
- Length
- 528 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidinol phosphatase
- EC
- 3.1.3.15
- UniProt
- Q5SLG2
- Ligands
- FE, ZN, PO4
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol phosphatase (EC 3.1.3.15) | protein | 263 | 44% helix, 19% strand | Q5SLG2 |
| B | Histidinol phosphatase (EC 3.1.3.15) | protein | 265 | 43% helix, 20% strand | Q5SLG2 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 4 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.59 | 0.83 | 24 | ZN, FE, PO4 |
| 2 | 180 | 0.58 | 0.82 | 29 | FE, PO4 |
| 3 | 234 | 0.57 | 0.79 | 35 | GOL |
| 4 | 56 | 0.28 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1021 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2YZ5 · Histidinol Phosphate Phosphatase complexed with Phosphate · 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 Q5SLG2
- Elsewhere: RCSB PDB 2YZ5 · PDBe 2YZ5 · UniProt Q5SLG2
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