Research workbench
Prolyl oligopeptidase from porcine brain, S554A mutant with bound peptide ligand gly-phe-arg-pro
Analyse Prolyl oligopeptidase from porcine brain, S554A mutant with bound peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UOO
- Type
- protein
- Length
- 714 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prolyl endopeptidase; Peptide ligand gly-phe-arg-pro
- EC
- 3.4.21.26
- UniProt
- P23687
- Pockets
- 6 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 22% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prolyl endopeptidase (EC 3.4.21.26) | protein | 710 | 22% helix, 33% strand | P23687 |
| B | Peptide ligand gly-phe-arg-pro | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- GOL · Glycerol · additive · 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 | 793 | 0.74 | 0.78 | 70 | empty |
| 2 | 849 | 0.74 | 0.78 | 79 | empty |
| 3 | 102 | 0.52 | 0.82 | 22 | empty |
| 4 | 78 | 0.38 | 0.77 | 17 | empty |
| 5 | 56 | 0.27 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 401 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1UOO · Prolyl oligopeptidase from porcine brain, S554A mutant with bound peptide ligand… · 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 1UOO · PDBe 1UOO · UniProt P23687
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.