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4UIS

The cryoEM structure of human gamma-Secretase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0016485biological_processprotein processing
B0016020cellular_componentmembrane
B0016485biological_processprotein processing
B0042500molecular_functionaspartic endopeptidase activity, intramembrane cleaving
G0003796molecular_functionlysozyme activity
G0003824molecular_functioncatalytic activity
G0009253biological_processpeptidoglycan catabolic process
G0016787molecular_functionhydrolase activity
G0016798molecular_functionhydrolase activity, acting on glycosyl bonds
G0016998biological_processcell wall macromolecule catabolic process
G0030430cellular_componenthost cell cytoplasm
G0031640biological_processkilling of cells of another organism
G0042742biological_processdefense response to bacterium
G0044659biological_processviral release from host cell by cytolysis
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. VAATrlDsRSFAWNV
ChainResidueDetails
AVAL277-VAL291

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:26280335
ChainResidueDetails
BILE408-UNK428
BUNK434-GLN454

site_idSWS_FT_FI2
Number of Residues3
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:26280335
ChainResidueDetails
BUNK429-UNK433
ATRP289
ALEU471
AGLU500
AILE555
AVAL579
AUNK620
AALA631

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ATHR209
ACYS213
ATYR453

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: 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
ChainResidueDetails
APRO423

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:30630874, ECO:0007744|PDB:6IYC
ChainResidueDetails
AGLN639

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19349973
ChainResidueDetails
AUNK671

237735

PDB entries from 2025-06-18

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