Research workbench
Mutant human cathepsin S with irreversible inhibitor cra-14013
Analyse Mutant human cathepsin S with irreversible inhibitor cra-14013 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FYE
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cathepsin S preproprotein
- EC
- 3.4.22.27
- UniProt
- P25774
- Ligands
- BCQ
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cathepsin S preproprotein (EC 3.4.22.27) | protein | 217 | 29% helix, 23% strand | P25774 |
Ligands and binding sites
- BCQ · N-[(1R)-1-[({[(5S)-3,5-dimethyl-2,5-dihydroisoxazol-4-yl]methyl}sulfonyl)methyl]-2-oxo-2-({(1S)-3-phenyl-1-[2-(phenylsulfonyl)ethyl]propyl}amino)ethyl]morpholine-4-carboxamide · 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 | 95 | 0.40 | 0.77 | 21 | BCQ |
Modifications
Observed in the structure: 3 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 2FYE · PDBe 2FYE · UniProt P25774
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