Research workbench
Crystal structure of human SHIP2 Phosphatase-C2 double mutant F593D/L597D
Analyse Crystal structure of human SHIP2 Phosphatase-C2 double mutant F593D/L597D in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OKP
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.85
- Source
- Homo sapiens
- Molecule
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
- EC
- 3.1.3.86
- UniProt
- O15357
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · resolution 1.85 · 1 distinct chain · 17% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) | protein | 421 | 17% helix, 40% strand | O15357 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.64 | 0.81 | 48 | EDO |
| 2 | 107 | 0.55 | 0.84 | 19 | empty |
| 3 | 64 | 0.32 | 0.75 | 20 | empty |
Compared structures
- 5OKP · Crystal structure of human SHIP2 phosphatase-C2 double mutant F593D/L597D · the same entry in another collection · chain A against A, TM-score 1.00
- O15357 · AlphaFold monomer V2.0 prediction for phosphatidylinositol 3,4,5-trisphosphate… · 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 O15357
- Elsewhere: RCSB PDB 5OKP · PDBe 5OKP · UniProt O15357
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