MolNFT v1 · #62309 · protein
Crystal structure of human PPPDE1
3EBQ · Molecule: PPPDE1 (permuted papain fold peptidases of dsrna…: “Crystal structure of human PPPDE1”. X-ray diffraction, 1 ligand (HG), 1 pocket (best druggability 0.56). MolNFT v1 #62309 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3EBQ
- Type
- protein
- Length
- 144 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Molecule: PPPDE1 (permuted papain fold peptidases of dsrna viruses and eukaryotes 1)…
- EC
- 3.4.22.-
- UniProt
- Q6ICB0
- Ligands
- HG
- Pockets
- 1 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Molecule: PPPDE1 (permuted papain fold peptidases of dsrna viruses and eukaryotes 1), UPF0326 protein FAM152B (EC 3.4.22.-) | protein | 144 | 38% helix, 23% strand | Q6ICB0 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.56 | 0.78 | 32 | HG |
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 Q6ICB0
- Elsewhere: RCSB PDB 3EBQ · PDBe 3EBQ · UniProt Q6ICB0
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