MolNFT v1 · #176307 · protein

Falcilysin in complex with mefloquine

7DIA: “Falcilysin in complex with mefloquine”. X-ray diffraction, 3 ligands (H8O, YMZ, ZN), 16 pockets (best druggability 0.82). MolNFT v1 #176307 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7DIA
Type: protein
Length: 1,072 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Falcilysin
UniProt: Q9U7N7
Ligands: H8O, YMZ, ZN
Pockets: 16 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Falcilysin	protein	1072	49% helix, 19% strand	Q9U7N7

Ligands and binding sites

H8O · (S)-[2,8-bis(trifluoromethyl)quinolin-4-yl]-[(2S)-piperidin-2-yl]methanol · ligand · chains A
YMZ · (11R,12S)- Mefloquine · ligand · chains A
ZN · Zinc ion · metal · chains A
EDO · 1,2-ethanediol · additive · 4 copies · chains A
ACT · Acetate ion · additive · 3 copies · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

16 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	954	0.82	0.84	111	EDO
2	769	0.78	0.82	63	ACT, EDO
3	668	0.70	0.78	57	ACT
4	528	0.64	0.76	52	H8O
5	136	0.57	0.83	30	GOL

Compared structures

7DIA · Falcilysin in complex with mefloquine · 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 7DIA · PDBe 7DIA · UniProt Q9U7N7

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