MolNFT v1 · #105630 · protein
Crystal structure of PPC2A-D38K
4RAG · Protein phosphatase 1A: “Crystal structure of PPC2A-D38K”. X-ray diffraction, 1 ligand (MN), 4 pockets (best druggability 0.45). MolNFT v1 #105630 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4RAG
- Type
- protein
- Length
- 362 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein phosphatase 1A
- EC
- 3.1.3.16
- UniProt
- P35813
- Ligands
- MN
- Pockets
- 4 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein phosphatase 1A (EC 3.1.3.16) | protein | 362 | 37% helix, 26% strand | P35813 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 105 | 0.45 | 0.79 | 16 | empty |
| 2 | 109 | 0.40 | 0.76 | 20 | empty |
| 3 | 74 | 0.35 | 0.76 | 14 | empty |
| 4 | 52 | 0.29 | 0.76 | 17 | empty |
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 P35813
- Elsewhere: RCSB PDB 4RAG · PDBe 4RAG · UniProt P35813
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