4NGE
Crystal Structure of Human Presequence Protease in Complex with Amyloid-beta (1-40)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004222 | molecular_function | metalloendopeptidase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0006508 | biological_process | proteolysis |
| A | 0006626 | biological_process | protein targeting to mitochondrion |
| A | 0008047 | molecular_function | enzyme activator activity |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016485 | biological_process | protein processing |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0016020 | cellular_component | membrane |
| D | 0004222 | molecular_function | metalloendopeptidase activity |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005759 | cellular_component | mitochondrial matrix |
| D | 0006508 | biological_process | proteolysis |
| D | 0006626 | biological_process | protein targeting to mitochondrion |
| D | 0008047 | molecular_function | enzyme activator activity |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016485 | biological_process | protein processing |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1101 |
| Chain | Residue |
| A | HIS104 |
| A | HIS108 |
| A | GLU205 |
| B | PHE20 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1102 |
| Chain | Residue |
| A | PHE168 |
| A | HIS254 |
| A | ALA255 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 1103 |
| Chain | Residue |
| A | ASP679 |
| D | ASP679 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 1104 |
| Chain | Residue |
| A | ASN777 |
| A | ARG779 |
| A | ILE839 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL D 1101 |
| Chain | Residue |
| D | ASP735 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL D 1102 |
| Chain | Residue |
| D | ASP413 |
| D | LYS494 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 101 |
| Chain | Residue |
| D | HIS104 |
| D | HIS108 |
| D | GLU205 |
| E | PHE20 |
| E | ALA21 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 60 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Compositional bias: {"description":"Basic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16849325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24931469","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q9LJL3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24931469","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4L3T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4NGE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8K411","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8K411","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by alpha-secretase","evidences":[{"source":"PubMed","id":"11851430","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage; by theta-secretase","evidences":[{"source":"PubMed","id":"16816112","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
