Research workbench
Dissecting and designing inhibitor selectivity determinants at the S1 site using an artificial ALA190 protease (ALA190 upa)
Analyse Dissecting and designing inhibitor selectivity determinants at the S1 site… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O5F
- Type
- protein
- Length
- 358 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine protease hepsin
- EC
- 3.4.21.-
- UniProt
- P05981
- Ligands
- CR9
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Serine protease hepsin (EC 3.4.21.-) | protein | 110 | 21% helix, 35% strand | P05981 |
| H | Serine protease hepsin (EC 3.4.21.-) | protein | 248 | 11% helix, 36% strand | P05981 |
Ligands and binding sites
- CR9 · 2-{5-[amino(iminio)methyl]-6-fluoro-1H-benzimidazol-2-yl}-6-[(2-methylcyclohexyl)oxy]benzenolate · ligand · chains H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 95 | 0.42 | 0.78 | 25 | empty |
| 2 | 57 | 0.39 | 0.81 | 15 | CR9 |
Interfaces
1 interface between chains.
- L–H · 1237 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 1O5F · Dissecting and Designing Inhibitor Selectivity Determinants at the S1 site Using an… · the same entry in another collection · chain L against L, TM-score 1.00
- P05981 · AlphaFold monomer V2.0 prediction for serine protease hepsin (P05981) · a predicted model of the same protein · chain L against A, TM-score 0.99
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 P05981
- Elsewhere: RCSB PDB 1O5F · PDBe 1O5F · UniProt P05981
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