Research workbench
PanDDA analysis group deposition -- PHIP in complex with Z1004277578
Analyse PanDDA analysis group deposition -- PHIP in complex with Z1004277578 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FVP
- Type
- protein
- Length
- 121 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.15
- Source
- Homo sapiens
- Molecule
- PH-interacting protein
- UniProt
- Q8WWQ0
- Ligands
- ZQ0
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · resolution 1.15 · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PH-interacting protein | protein | 121 | 68% helix, 0% strand | Q8WWQ0 |
Ligands and binding sites
- ZQ0 · N-butyl-4-(5-methylfuran-2-carbonyl)piperazine-1-carboxamide · 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 | 125 | 0.55 | 0.83 | 22 | ZQ0 |
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 Q8WWQ0
- Elsewhere: RCSB PDB 7FVP · PDBe 7FVP · UniProt Q8WWQ0
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