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Crystal structures of falcilysin, a M16 metalloprotease from the malaria parasite plasmodium falciparum

Analyse Crystal structures of falcilysin, a M16 metalloprotease from the malaria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3S5H
Type
protein
Length
1,078 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Falcilysin
UniProt
Q76NL8
Ligands
CO
Pockets
19 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFalcilysinprotein107848% helix, 19% strandQ76NL8

Ligands and binding sites

  • CO · Cobalt (II) ion · metal · chains A

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

Pockets

19 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111860.850.86147empty
24690.680.7942empty
31870.610.8325empty
43380.590.7729empty
52040.570.8043empty

Compared structures

  • 3S5H · Crystal structures of falcilysin, a M16 metalloprotease from the malaria parasite… · the same entry in another collection · chain A against A, TM-score 1.00

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