Research workbench
Prolyl oligopeptidase with GSK552
Analyse Prolyl oligopeptidase with GSK552 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DDU
- Type
- protein
- Length
- 707 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prolyl endopeptidase
- EC
- 3.4.21.26
- UniProt
- P48147
- Ligands
- 552
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl endopeptidase (EC 3.4.21.26) | protein | 707 | 23% helix, 33% strand | P48147 |
Ligands and binding sites
- 552 · (6S)-1-chloro-3-[(4-fluorobenzyl)oxy]-6-(pyrrolidin-1-ylcarbonyl)pyrrolo[1,2-a]pyrazin-4(6H)-one · ligand · chains A
- ACT · Acetate ion · additive · 5 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 839 | 0.76 | 0.79 | 92 | ACT |
| 2 | 743 | 0.72 | 0.78 | 73 | ACT, 552 |
| 3 | 104 | 0.53 | 0.83 | 24 | empty |
| 4 | 76 | 0.38 | 0.77 | 25 | ACT |
| 5 | 79 | 0.38 | 0.77 | 16 | 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 P48147
- Elsewhere: RCSB PDB 3DDU · PDBe 3DDU · UniProt P48147
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