Research workbench
Prolyl oligopeptidase from porcine brain, Y73C/V427C/C255T mutant
Analyse Prolyl oligopeptidase from porcine brain, Y73C/V427C/C255T mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VZ2
- Type
- protein
- Length
- 710 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prolyl endopeptidase
- EC
- 3.4.21.26
- UniProt
- P23687
- Pockets
- 9 · best druggability 0.73
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 | 710 | 23% helix, 33% strand | P23687 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 572 | 0.73 | 0.81 | 63 | empty |
| 2 | 295 | 0.65 | 0.81 | 34 | empty |
| 3 | 163 | 0.54 | 0.80 | 36 | GOL |
| 4 | 101 | 0.51 | 0.82 | 25 | empty |
| 5 | 71 | 0.34 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 1 covalent, 1 disulfide (additive adduct, disulfide).
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 1VZ2 · PDBe 1VZ2 · UniProt P23687
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