Research workbench
Prolyl oligopeptidase from porcine muscle
Analyse Prolyl oligopeptidase from porcine muscle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QFM
- Type
- protein
- Length
- 710 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (prolyl oligopeptidase)
- EC
- 3.4.21.26
- UniProt
- P23687
- Ligands
- SGL
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (prolyl oligopeptidase) (EC 3.4.21.26) | protein | 710 | 23% helix, 33% strand | P23687 |
Ligands and binding sites
- SGL · 1-hydroxy-1-thio-glycerol · ligand · 2 copies · chains A
- GOL · Glycerol · additive · 4 copies · chains A
- SGM · Monothioglycerol · additive · 2 copies · chains A
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 | 756 | 0.74 | 0.79 | 70 | empty |
| 2 | 508 | 0.67 | 0.78 | 40 | SGM |
| 3 | 344 | 0.60 | 0.77 | 54 | SGL |
| 4 | 89 | 0.49 | 0.82 | 26 | empty |
| 5 | 86 | 0.38 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 5 modified, 3 covalent (oxidation, additive adduct, covalent ligand).
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 P23687
- Elsewhere: RCSB PDB 1QFM · PDBe 1QFM · UniProt P23687
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