MolNFT v1 · #16140 · protein
Crystal structures of cathepsin S inhibitor complexes
1NPZ: “Crystal structures of cathepsin S inhibitor complexes”. X-ray diffraction, 1 ligand (C1P), 3 pockets (best druggability 0.66). MolNFT v1 #16140 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1NPZ
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin S
- EC
- 3.4.22.27
- UniProt
- P25774
- Ligands
- C1P
- Pockets
- 3 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cathepsin S (EC 3.4.22.27) | protein | 217 | 30% helix, 23% strand | P25774 |
Ligands and binding sites
- C1P · N~2~-(morpholin-4-ylcarbonyl)-N-[(3S)-1-phenyl-5-(phenylsulfonyl)pentan-3-yl]-L-leucinamide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 326 | 0.66 | 0.81 | 35 | empty |
| 2 | 244 | 0.54 | 0.77 | 27 | empty |
| 3 | 76 | 0.34 | 0.75 | 19 | C1P |
Interfaces
1 interface between chains.
- A–B · 751 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 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 1NPZ · PDBe 1NPZ · UniProt P25774
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