Research workbench
Falcilysin in complex with chloroquine
Analyse Falcilysin in complex with chloroquine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DI7
- Type
- protein
- Length
- 1,076 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Falcilysin
- UniProt
- Q9U7N7
- Ligands
- CLQ, ZN
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Falcilysin | protein | 1076 | 49% helix, 19% strand | Q9U7N7 |
Ligands and binding sites
- CLQ · N4-(7-chloro-quinolin-4-yl)-N1,N1-diethyl-pentane-1,4-diamine · ligand · chains A
- ZN · Zinc ion · metal · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 522 | 0.80 | 0.87 | 66 | empty |
| 2 | 353 | 0.78 | 0.88 | 61 | empty |
| 3 | 843 | 0.74 | 0.78 | 81 | ACT |
| 4 | 142 | 0.60 | 0.84 | 25 | ACT |
| 5 | 335 | 0.57 | 0.76 | 30 | CLQ |
Compared structures
- 7DI7 · Falcilysin in complex with chloroquine · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9U7N7
- Elsewhere: RCSB PDB 7DI7 · PDBe 7DI7 · UniProt Q9U7N7
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