MolNFT v1 · #159020 · protein
PP1 Y134K
6OBS · SERINE/THREONINE-protein phosphatase PP1-alpha catalytic…: “PP1 Y134K”. X-ray diffraction, 2 ligands (MN, PO4), 5 pockets (best druggability 0.57). MolNFT v1 #159020 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6OBS
- Type
- protein
- Length
- 586 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein phosphatase PP1-alpha catalytic subunit
- EC
- 3.1.3.16
- UniProt
- P62136
- Ligands
- MN, PO4
- Pockets
- 5 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | SERINE/THREONINE-protein phosphatase PP1-alpha catalytic subunit (EC 3.1.3.16) | protein | 293 | 33% helix, 19% strand | P62136 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.57 | 0.82 | 33 | empty |
| 2 | 153 | 0.48 | 0.77 | 20 | empty |
| 3 | 108 | 0.48 | 0.80 | 17 | empty |
| 4 | 123 | 0.44 | 0.76 | 20 | empty |
| 5 | 52 | 0.27 | 0.74 | 15 | MN, PO4 |
Interfaces
1 interface between chains.
- A–B · 726 Ų buried · 13 hydrogen bonds · protein-protein
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 P62136
- Elsewhere: RCSB PDB 6OBS · PDBe 6OBS · UniProt P62136
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