Research workbench
The structural basis of pten regulation by multi-site phosphorylation
Analyse The structural basis of pten regulation by multi-site phosphorylation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JTX
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein…
- EC
- 3.1.3.16, 3.1.3.48, 3.1.3.67
- Pockets
- 2 · best druggability 0.37
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase pten (EC 3.1.3.16, 3.1.3.48, 3.1.3.67) | protein | 279 | 27% helix, 33% strand | — |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.37 | 0.79 | 13 | empty |
| 2 | 109 | 0.34 | 0.72 | 20 | empty |
Compared structures
- 7JTX · the structural basis of PTEN regulation by multi-site phosphorylation · 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
- Elsewhere: RCSB PDB 7JTX · PDBe 7JTX
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