Research workbench
Crystal structure of protein phosphatase 2A bound to tiprl
Analyse Crystal structure of protein phosphatase 2A bound to tiprl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W0W
- Type
- protein
- Length
- 4,375 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein phosphatase 2A 65 kda regulatory subunit a alpha isoform…
- EC
- 3.1.3.16
- UniProt
- P30153, Q8BH58, P67775
- Ligands
- MN
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 8 distinct chains · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | SERINE/THREONINE-protein phosphatase 2A 65 kda regulatory subunit a alpha isoform | protein | 582 | 74% helix, 0% strand | P30153 |
| B | TIP41-like protein | protein | 216 | 16% helix, 43% strand | Q8BH58 |
| C | SERINE/THREONINE-protein phosphatase 2A catalytic subunit alpha isoform (EC 3.1.3.16) | protein | 298 | 35% helix, 17% strand | P67775 |
| E | TIP41-like protein | protein | 215 | 15% helix, 41% strand | Q8BH58 |
| F, I, L | SERINE/THREONINE-protein phosphatase 2A catalytic subunit alpha isoform (EC 3.1.3.16) | protein | 296 | 30% helix, 16% strand | P67775 |
| G | SERINE/THREONINE-protein phosphatase 2A 65 kda regulatory subunit a alpha isoform | protein | 584 | 75% helix, 0% strand | P30153 |
| H, K | TIP41-like protein | protein | 215 | 13% helix, 45% strand | Q8BH58 |
| J | SERINE/THREONINE-protein phosphatase 2A 65 kda regulatory subunit a alpha isoform | protein | 580 | 68% helix, 0% strand | P30153 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 4 copies · chains C, F, I, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 990 | 0.77 | 0.79 | 90 | empty |
| 2 | 74 | 0.74 | 0.97 | 20 | empty |
| 3 | 1150 | 0.73 | 0.77 | 120 | empty |
| 4 | 615 | 0.71 | 0.79 | 51 | empty |
| 5 | 712 | 0.69 | 0.77 | 62 | empty |
Interfaces
23 interfaces between chains.
- G–I · 1137 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 1092 Ų buried · 20 hydrogen bonds · protein-protein
- J–L · 1052 Ų buried · 17 hydrogen bonds · protein-protein
- G–J · 1047 Ų buried · 11 hydrogen bonds · protein-protein
- D–F · 1033 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 56 modified (engineered).
Compared structures
- 5W0W · Crystal structure of Protein Phosphatase 2A bound to TIPRL · the same entry in another collection · chain L against L, TM-score 1.00
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 P30153
- Every structure of UniProt Q8BH58
- Every structure of UniProt P67775
- Elsewhere: RCSB PDB 5W0W · PDBe 5W0W · UniProt P30153 · UniProt Q8BH58 · UniProt P67775
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