Research workbench
Prolyl oligopeptidase from porcine muscle with covalently bound inhibitor Z-pro-prolinal
Analyse Prolyl oligopeptidase from porcine muscle with covalently bound inhibitor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QFS
- 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
- ZPR
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 22% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (prolyl oligopeptidase) (EC 3.4.21.26) | protein | 710 | 22% helix, 33% strand | P23687 |
Ligands and binding sites
- ZPR · N-benzyloxycarbonyl-L-prolyl-L-prolinal · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 758 | 0.74 | 0.79 | 71 | empty |
| 2 | 429 | 0.67 | 0.79 | 37 | empty |
| 3 | 272 | 0.55 | 0.76 | 33 | ZPR |
| 4 | 95 | 0.49 | 0.82 | 25 | empty |
| 5 | 100 | 0.40 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1QFS · Prolyl oligopeptidase from porcine muscle with covalently bound inhibitor Z-pro-prolinal · the same entry in another collection · chain A against A, TM-score 1.00
- P23687 · AlphaFold monomer V2.0 prediction for prolyl endopeptidase (P23687) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 1QFS · PDBe 1QFS · UniProt P23687
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