MolNFT v1 · #16152 · protein
Crystal structures of cathepsin S inhibitor complexes
1NQC: “Crystal structures of cathepsin S inhibitor complexes”. X-ray diffraction, 1 ligand (C4P), 1 pocket (best druggability 0.39). MolNFT v1 #16152 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NQC
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin S
- EC
- 3.4.22.27
- UniProt
- P25774
- Ligands
- C4P
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin S (EC 3.4.22.27) | protein | 217 | 29% helix, 24% strand | P25774 |
Ligands and binding sites
- C4P · N-[(1R)-2-(benzylsulfanyl)-1-formylethyl]-N-(morpholin-4-ylcarbonyl)-L-phenylalaninamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.39 | 0.76 | 22 | C4P |
Modifications
Observed in the structure: 2 disulfide, 1 covalent (disulfide, covalent ligand).
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 P25774
- Elsewhere: RCSB PDB 1NQC · PDBe 1NQC · UniProt P25774
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.