7DI7
Falcilysin in complex with chloroquine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004222 | molecular_function | metalloendopeptidase activity |
A | 0005773 | cellular_component | vacuole |
A | 0005774 | cellular_component | vacuolar membrane |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0009536 | cellular_component | plastid |
A | 0016020 | cellular_component | membrane |
A | 0016485 | biological_process | protein processing |
A | 0016787 | molecular_function | hydrolase activity |
A | 0020011 | cellular_component | apicoplast |
A | 0020020 | cellular_component | food vacuole |
A | 0031982 | cellular_component | vesicle |
A | 0042540 | biological_process | hemoglobin catabolic process |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 36 |
Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10096","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2011","submissionDatabase":"PDB data bank","title":"Crystal structures of falcilysin, a M16 metalloprotease from the malaria parasite Plasmodium falciparum.","authors":["Morgunova E.","Ponpuak M.","Istvan E.","Popov A.","Goldberg D.","Eneqvist T."]}},{"source":"PDB","id":"3S5K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3S5M","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |