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 | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:16849325, ECO:0000269|PubMed:24931469 |
| Chain | Residue | Details |
| D | GLN107 | |
| B | HIS14 | |
| E | HIS6 | |
| E | HIS14 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q9LJL3 |
| Chain | Residue | Details |
| D | GLU180 | |
| E | TYR10 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24931469, ECO:0007744|PDB:4L3T, ECO:0007744|PDB:4NGE |
| Chain | Residue | Details |
| D | HIS104 | |
| D | HIS108 | |
| D | GLU205 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q8K411 |
| Chain | Residue | Details |
| D | LYS759 | |
| D | MLY884 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q8K411 |
| Chain | Residue | Details |
| D | LYS770 | |
| E | ASP7 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8K411 |
| Chain | Residue | Details |
| D | LYS849 | |
| D | MLY946 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by theta-secretase => ECO:0000269|PubMed:16816112 |
| Chain | Residue | Details |
| B | PHE19 | |
| E | PHE19 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | SITE: Implicated in free radical propagation => ECO:0000250 |
| Chain | Residue | Details |
| B | GLY33 | |
| E | GLY33 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | SITE: Susceptible to oxidation => ECO:0000269|PubMed:10535332 |
| Chain | Residue | Details |
| B | MET35 | |
| E | MET35 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by gamma-secretase; site 1 => ECO:0000305|PubMed:11851430 |
| Chain | Residue | Details |
| B | VAL40 | |
| E | VAL40 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (HexNAc...) tyrosine; partial => ECO:0000269|PubMed:22576872 |
| Chain | Residue | Details |
| B | TYR10 | |
| E | TYR10 |
