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Crystal structure of the pten tumor suppressor
Analyse Crystal structure of the pten tumor suppressor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1D5R
- Type
- protein
- Length
- 307 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoinositide phosphatase pten
- EC
- 3.1.3.48
- UniProt
- P60484
- Pockets
- 4 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoinositide phosphatase pten (EC 3.1.3.48) | protein | 307 | 26% helix, 33% strand | P60484 |
Ligands and binding sites
- TLA · L(+)-tartaric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.40 | 0.77 | 17 | empty |
| 2 | 52 | 0.36 | 0.80 | 15 | TLA |
| 3 | 77 | 0.30 | 0.73 | 14 | empty |
| 4 | 51 | 0.28 | 0.75 | 16 | empty |
Compared structures
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 1D5R · PDBe 1D5R · UniProt P60484
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