Research workbench
Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1
Analyse Crystal structure of the tumor-promoter okadaic acid bound to protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JK7
- Type
- protein
- Length
- 294 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE protein phosphatase PP1-gamma catalytic subunit
- EC
- 3.1.3.16
- UniProt
- P36873
- Ligands
- OKA, MN, SO4
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE protein phosphatase PP1-gamma catalytic subunit (EC 3.1.3.16) | protein | 294 | 34% helix, 19% strand | P36873 |
Ligands and binding sites
- OKA · Okadaic acid · ligand · chains A
- MN · Manganese (II) ion · metal · 2 copies · chains A
- SO4 · Sulfate ion · ion · chains A
- BME · Beta-mercaptoethanol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 97 | 0.34 | 0.74 | 18 | empty |
| 2 | 51 | 0.30 | 0.76 | 13 | empty |
Compared structures
- 1JK7 · Crystal structure of the tumor-promoter okadaic acid bound to protein phosphatase-1 · the same entry in another collection · chain A against A, TM-score 1.00
- P36873 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase PP1-gamma… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P36873
- Elsewhere: RCSB PDB 1JK7 · PDBe 1JK7 · UniProt P36873
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