Research workbench
Crystal structure of engineered neurolysin with thimet oligopeptidase specificity for neurotensin cleavage site.
Analyse Crystal structure of engineered neurolysin with thimet oligopeptidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O3E
- Type
- protein
- Length
- 665 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neurolysin
- EC
- 3.4.24.16
- UniProt
- P42676
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neurolysin (EC 3.4.24.16) | protein | 665 | 59% helix, 8% strand | P42676 |
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
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 991 | 0.77 | 0.79 | 82 | empty |
| 2 | 680 | 0.74 | 0.80 | 71 | empty |
| 3 | 57 | 0.38 | 0.80 | 16 | empty |
| 4 | 53 | 0.37 | 0.80 | 17 | empty |
| 5 | 75 | 0.31 | 0.74 | 21 | empty |
Compared structures
- 2O3E · Crystal structure of engineered neurolysin with thimet oligopeptidase specificity for… · the same entry in another collection · chain A against A, TM-score 1.00
- P42676 · AlphaFold monomer V2.0 prediction for neurolysin, mitochondrial (P42676) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P42676
- Elsewhere: RCSB PDB 2O3E · PDBe 2O3E · UniProt P42676
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