Research workbench
Crystal structure of a complex between protein phosphatase 1 alpha (PP1) and the PP1 binding and PDZ domains of spinophilin
Analyse Crystal structure of a complex between protein phosphatase 1 alpha (PP1) and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EGG
- Type
- protein
- Length
- 814 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein phosphatase PP1-alpha catalytic subunit; Spinophilin
- EC
- 3.1.3.16
- UniProt
- P62136, O35274
- Ligands
- MN
- Pockets
- 8 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 28% helix, 24% 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 | 294 | 35% helix, 20% strand | P62136 |
| C | Spinophilin | protein | 160 | 18% helix, 33% strand | O35274 |
| D | Spinophilin | protein | 66 | 17% helix, 18% strand | O35274 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains A, B
- GOL · Glycerol · additive · 7 copies · chains A, B, C, D
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 681 | 0.68 | 0.76 | 58 | empty |
| 2 | 287 | 0.60 | 0.79 | 29 | empty |
| 3 | 92 | 0.44 | 0.80 | 21 | empty |
| 4 | 146 | 0.42 | 0.75 | 21 | empty |
| 5 | 64 | 0.38 | 0.79 | 13 | empty |
Interfaces
4 interfaces between chains.
- B–D · 2079 Ų buried · 40 hydrogen bonds · protein-protein
- A–C · 2065 Ų buried · 39 hydrogen bonds · protein-protein
- A–B · 424 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 396 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3EGG · Crystal structure of a complex between Protein Phosphatase 1 alpha (PP1) and the PP1… · the same entry in another collection · chain D against D, TM-score 1.00
- 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 1.00
- O35274 · AlphaFold monomer V2.0 prediction for neurabin-2 (O35274) · a predicted model of the same protein · chain C against A, TM-score 0.94
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 O35274
- Elsewhere: RCSB PDB 3EGG · PDBe 3EGG · UniProt P62136 · UniProt O35274
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