MolNFT v1 · #129448 · protein
Crystal structure of human SHIP2 phosphatase-C2 double mutant F593D/L597D
5OKO · Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2: “Crystal structure of human SHIP2 phosphatase-C2 double mutant F593D/L597D”. X-ray diffraction, 8 pockets (best druggability 0.65). MolNFT v1 #129448 on GenesisL1: 3D…
- PDB
- 5OKO
- Type
- protein
- Length
- 853 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
- EC
- 3.1.3.86
- UniProt
- O15357
- Pockets
- 8 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 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 | 427 | 17% helix, 41% strand | O15357 |
| B | Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 (EC 3.1.3.86) | protein | 426 | 16% helix, 40% strand | O15357 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
- B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.65 | 0.80 | 52 | EDO |
| 2 | 331 | 0.60 | 0.78 | 48 | EDO |
| 3 | 84 | 0.53 | 0.84 | 18 | empty |
| 4 | 73 | 0.53 | 0.85 | 17 | empty |
| 5 | 66 | 0.42 | 0.81 | 17 | empty |
Compared structures
- 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 0.99
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 5OKO · PDBe 5OKO · UniProt O15357
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