Research workbench
Structure of PP1 alpha phosphatase bound to ASPP2
Analyse Structure of PP1 alpha phosphatase bound to ASPP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GHM
- Type
- protein
- Length
- 996 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein phosphatase PP1-alpha catalytic subunit; Apoptosis-stimulating…
- EC
- 3.1.3.16
- UniProt
- P62136, Q13625
- Ligands
- MN
- Pockets
- 7 · best druggability 0.58
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein phosphatase PP1-alpha catalytic subunit (EC 3.1.3.16) | protein | 297 | 32% helix, 19% strand | P62136 |
| B | SERINE/THREONINE-protein phosphatase PP1-alpha catalytic subunit (EC 3.1.3.16) | protein | 294 | 34% helix, 19% strand | P62136 |
| C | Apoptosis-stimulating of P53 protein 2 | protein | 202 | 37% helix, 14% strand | Q13625 |
| D | Apoptosis-stimulating of P53 protein 2 | protein | 203 | 37% helix, 15% strand | Q13625 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 12 copies · chains A, B, C, D
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 6 copies · chains A, B, C, D
- GOL · Glycerol · additive · 4 copies · chains A, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.58 | 0.78 | 35 | GOL |
| 2 | 280 | 0.58 | 0.78 | 35 | EDO |
| 3 | 60 | 0.40 | 0.80 | 15 | empty |
| 4 | 84 | 0.37 | 0.76 | 23 | empty |
| 5 | 67 | 0.32 | 0.75 | 12 | NHE |
Interfaces
3 interfaces between chains.
- A–D · 1334 Ų buried · 27 hydrogen bonds · protein-protein
- B–C · 1321 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 328 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6GHM · Structure of PP1 alpha phosphatase bound to ASPP2 · the same entry in another collection · chain D against D, TM-score 1.00
- Q13625 · AlphaFold monomer V2.0 prediction for apoptosis-stimulating of P53 protein 2 (Q13625) · a predicted model of the same protein · chain D against A, TM-score 0.99
- P62136 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase PP1-alpha… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P62136
- Every structure of UniProt Q13625
- Elsewhere: RCSB PDB 6GHM · PDBe 6GHM · UniProt P62136 · UniProt Q13625
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