Research workbench
Crystal structure of wt PPM1H phosphatase
Analyse Crystal structure of wt PPM1H phosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L4J
- Type
- protein
- Length
- 789 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
- 6 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein phosphatase 1H (EC 3.1.3.16) | protein | 395 | 33% helix, 26% strand | Q9ULR3 |
| B | Protein phosphatase 1H (EC 3.1.3.16) | protein | 394 | 32% helix, 26% 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
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 925 | 0.72 | 0.76 | 75 | empty |
| 2 | 309 | 0.53 | 0.75 | 45 | empty |
| 3 | 245 | 0.53 | 0.76 | 30 | MG |
| 4 | 86 | 0.40 | 0.78 | 22 | empty |
| 5 | 70 | 0.37 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1456 Ų buried · 10 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 Q9ULR3
- Elsewhere: RCSB PDB 7L4J · PDBe 7L4J · UniProt Q9ULR3
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