Research workbench
Crystal structure of human phosphatase pten in its reduced state
Analyse Crystal structure of human phosphatase pten in its reduced state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BZZ
- Type
- protein
- Length
- 1,256 residues
- Chains
- 4
- 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
- Pockets
- 15 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | 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, 32% strand | P60484 |
Ligands and binding sites
- TLA · L(+)-tartaric acid · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 729 | 0.75 | 0.80 | 77 | empty |
| 2 | 753 | 0.75 | 0.80 | 75 | empty |
| 3 | 814 | 0.75 | 0.79 | 68 | empty |
| 4 | 194 | 0.48 | 0.75 | 24 | empty |
| 5 | 204 | 0.47 | 0.74 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–B · 826 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 622 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 618 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5BZZ · Crystal structure of human phosphatase PTEN in its reduced state · 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 5BZZ · PDBe 5BZZ · UniProt P60484
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