Research workbench
Crystal structure of engineered thimet oligopeptidase with neurolysin specificity in neurotensin cleavage site
Analyse Crystal structure of engineered thimet oligopeptidase with neurolysin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O36
- Type
- protein
- Length
- 654 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thimet oligopeptidase
- EC
- 3.4.24.15
- UniProt
- P52888
- Ligands
- ZN
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 61% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thimet oligopeptidase (EC 3.4.24.15) | protein | 654 | 61% helix, 8% strand | P52888 |
Ligands and binding sites
- ZN · Zinc ion · metal · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 791 | 0.74 | 0.79 | 71 | empty |
| 2 | 965 | 0.73 | 0.76 | 78 | empty |
| 3 | 79 | 0.43 | 0.80 | 17 | empty |
| 4 | 55 | 0.40 | 0.81 | 17 | empty |
| 5 | 61 | 0.35 | 0.78 | 15 | empty |
Compared structures
- 2O36 · Crystal structure of engineered thimet oligopeptidase with neurolysin specificity in… · the same entry in another collection · chain A against A, TM-score 1.00
- P52888 · AlphaFold monomer V2.0 prediction for thimet oligopeptidase (P52888) · a predicted model of the same protein · chain A against A, TM-score 0.88
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 P52888
- Elsewhere: RCSB PDB 2O36 · PDBe 2O36 · UniProt P52888
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