Research workbench
Yeast diphosphoinositol polyphosphate phosphohydrolase DDP1 mutation E80Q in complex with 1-INSP7
Analyse Yeast diphosphoinositol polyphosphate phosphohydrolase DDP1 mutation E80Q in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AUJ
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diphosphoinositol polyphosphate phosphohydrolase DDP1
- EC
- 3.6.1.52, 3.6.1.60
- UniProt
- Q99321
- Ligands
- O81, MG
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 21% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diphosphoinositol polyphosphate phosphohydrolase DDP1 (EC 3.6.1.52, 3.6.1.60) | protein | 158 | 21% helix, 37% strand | Q99321 |
Ligands and binding sites
- O81 · (1S,2R,3R,4S,5S,6R)-2,3,4,5,6-pentakis(phosphonooxy) cyclohexyl trihydrogen diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 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 | 130 | 0.39 | 0.75 | 30 | O81, MG |
Compared structures
- 7AUJ · Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 mutation E80Q in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99321 · AlphaFold monomer V2.0 prediction for diphosphoinositol polyphosphate phosphohydrolase… · a predicted model of the same protein · chain A against A, TM-score 0.88
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 Q99321
- Elsewhere: RCSB PDB 7AUJ · PDBe 7AUJ · UniProt Q99321
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