Research workbench
Achiral, cheap and potent inhibitors of plasmepsins II
Analyse Achiral, cheap and potent inhibitors of plasmepsins II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IGX
- Type
- protein
- Length
- 329 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Plasmepsin-2
- EC
- 3.4.23.39
- UniProt
- P46925
- Ligands
- A1T
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Plasmepsin-2 (EC 3.4.23.39) | protein | 329 | 13% helix, 48% strand | P46925 |
Ligands and binding sites
- A1T · 5-pentyl-N-{[4'-(piperidin-1-ylcarbonyl)biphenyl-4-yl]methyl}-N-[1-(pyridin-2-ylmethyl)piperidin-4-yl]pyridine-2-carboxamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.63 | 0.79 | 39 | A1T |
| 2 | 129 | 0.48 | 0.79 | 20 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P46925
- Elsewhere: RCSB PDB 2IGX · PDBe 2IGX · UniProt P46925
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