Research workbench
Structure of wild-type PPM1H phosphatase at 3.1 ångström resolution
Analyse Structure of wild-type PPM1H phosphatase at 3.1 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KPR
- Type
- protein
- Length
- 794 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein phosphatase 1H
- EC
- 3.1.3.16
- UniProt
- Q9ULR3
- Ligands
- MG
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein phosphatase 1H (EC 3.1.3.16) | protein | 403 | 31% helix, 25% strand | Q9ULR3 |
| B | Protein phosphatase 1H (EC 3.1.3.16) | protein | 391 | 30% helix, 27% strand | Q9ULR3 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 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 | 853 | 0.70 | 0.76 | 71 | empty |
| 2 | 267 | 0.54 | 0.77 | 33 | MG |
| 3 | 150 | 0.46 | 0.77 | 26 | MG |
| 4 | 112 | 0.41 | 0.76 | 22 | empty |
| 5 | 87 | 0.35 | 0.75 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1644 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 7KPR · Structure of wild-type PPM1H phosphatase at 3.1 Angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ULR3 · AlphaFold monomer V2.0 prediction for protein phosphatase 1H (Q9ULR3) · a predicted model of the same protein · chain B 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 Q9ULR3
- Elsewhere: RCSB PDB 7KPR · PDBe 7KPR · UniProt Q9ULR3
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