4UIS
The cryoEM structure of human gamma-Secretase complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016020 | cellular_component | membrane |
A | 0016485 | biological_process | protein processing |
B | 0016020 | cellular_component | membrane |
B | 0016485 | biological_process | protein processing |
B | 0042500 | molecular_function | aspartic endopeptidase activity, intramembrane cleaving |
G | 0003796 | molecular_function | lysozyme activity |
G | 0003824 | molecular_function | catalytic activity |
G | 0009253 | biological_process | peptidoglycan catabolic process |
G | 0016787 | molecular_function | hydrolase activity |
G | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
G | 0016998 | biological_process | cell wall macromolecule catabolic process |
G | 0030430 | cellular_component | host cell cytoplasm |
G | 0031640 | biological_process | killing of cells of another organism |
G | 0042742 | biological_process | defense response to bacterium |
G | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PROSITE/UniProt
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. VAATrlDsRSFAWNV |
Chain | Residue | Details |
A | VAL277-VAL291 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:26280335 |
Chain | Residue | Details |
B | ILE408-UNK428 | |
B | UNK434-GLN454 |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26280335 |
Chain | Residue | Details |
B | UNK429-UNK433 | |
A | TRP289 | |
A | LEU471 | |
A | GLU500 | |
A | ILE555 | |
A | VAL579 | |
A | UNK620 | |
A | ALA631 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | THR209 | |
A | CYS213 | |
A | TYR453 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:26280335, ECO:0000269|PubMed:30598546, ECO:0000269|PubMed:30630874, ECO:0007744|PDB:5A63, ECO:0007744|PDB:6IDF, ECO:0007744|PDB:6IYC |
Chain | Residue | Details |
A | PRO423 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30630874, ECO:0007744|PDB:6IYC |
Chain | Residue | Details |
A | GLN639 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973 |
Chain | Residue | Details |
A | UNK671 |