MolNFT v1 · #179122 · protein
Crystal structure of pten (aa 7-353 followed by spacer tgggsggtgggsggtgggcy ligated to peptide psdptptdpsdpenepfded)
7JVX · Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and…: “Crystal structure of pten (aa 7-353 followed by spacer tgggsggtgggsggtgggcy ligated to peptide…”. X-ray diffraction, 1 ligand (PO4), 3 pockets (best druggability 0.59).…
- PDB
- 7JVX
- Type
- protein
- Length
- 314 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
- UniProt
- P60484
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 31% 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 | 314 | 25% helix, 31% strand | P60484 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 239 | 0.59 | 0.80 | 37 | empty |
| 2 | 131 | 0.40 | 0.74 | 19 | empty |
| 3 | 82 | 0.37 | 0.76 | 16 | empty |
Compared structures
- 7JVX · Crystal structure of PTEN (aa 7-353 followed by spacer TGGGSGGTGGGSGGTGGGCY ligated to… · the same entry in another collection · chain A against A, TM-score 1.00
- P60484 · 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 P60484
- Elsewhere: RCSB PDB 7JVX · PDBe 7JVX · UniProt P60484
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