Research workbench
Crystal structure of neprilysin in complex with sampatrilat-asp.
Analyse Crystal structure of neprilysin in complex with sampatrilat-asp. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SVY
- Type
- protein
- Length
- 697 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neprilysin
- EC
- 3.4.24.11
- UniProt
- P08473
- Ligands
- D0W, NAG, ZN
- Pockets
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 59% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neprilysin (EC 3.4.24.11) | protein | 697 | 59% helix, 8% strand | P08473 |
Ligands and binding sites
- D0W · Sampatrilat-Asp · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1176 | 0.76 | 0.78 | 137 | D0W |
| 2 | 82 | 0.54 | 0.85 | 19 | empty |
| 3 | 132 | 0.45 | 0.77 | 25 | empty |
| 4 | 118 | 0.42 | 0.76 | 20 | empty |
| 5 | 78 | 0.36 | 0.77 | 14 | empty |
Modifications
Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).
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 P08473
- Elsewhere: RCSB PDB 6SVY · PDBe 6SVY · UniProt P08473
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