3NSJ
The X-ray crystal structure of lymphocyte perforin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001771 | biological_process | immunological synapse formation |
A | 0001772 | cellular_component | immunological synapse |
A | 0001909 | biological_process | leukocyte mediated cytotoxicity |
A | 0001913 | biological_process | T cell mediated cytotoxicity |
A | 0002357 | biological_process | defense response to tumor cell |
A | 0002418 | biological_process | immune response to tumor cell |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005764 | cellular_component | lysosome |
A | 0005768 | cellular_component | endosome |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0009306 | biological_process | protein secretion |
A | 0016020 | cellular_component | membrane |
A | 0017038 | biological_process | protein import |
A | 0022829 | molecular_function | wide pore channel activity |
A | 0031410 | cellular_component | cytoplasmic vesicle |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0031904 | cellular_component | endosome lumen |
A | 0042802 | molecular_function | identical protein binding |
A | 0044194 | cellular_component | cytolytic granule |
A | 0046872 | molecular_function | metal ion binding |
A | 0051260 | biological_process | protein homooligomerization |
A | 0051607 | biological_process | defense response to virus |
A | 0051712 | biological_process | positive regulation of killing of cells of another organism |
A | 0071806 | biological_process | protein transmembrane transport |
A | 0140507 | biological_process | granzyme-mediated programmed cell death signaling pathway |
A | 0140911 | molecular_function | pore-forming activity |
Functional Information from PROSITE/UniProt
site_id | PS00279 |
Number of Residues | 12 |
Details | MACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YhelissYGTHF |
Chain | Residue | Details |
A | TYR211-PHE222 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 20 |
Details | TRANSMEM: Beta stranded; Name=CH1 => ECO:0000305|PubMed:21037563 |
Chain | Residue | Details |
A | TRP128-GLY148 |
site_id | SWS_FT_FI2 |
Number of Residues | 22 |
Details | TRANSMEM: Beta stranded; Name=CH2 => ECO:0000305|PubMed:21037563 |
Chain | Residue | Details |
A | CYS256-CYS278 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26306037, ECO:0007744|PDB:4Y1T |
Chain | Residue | Details |
A | GLY428 | |
A | THR432 | |
A | ALA433 | |
A | GLU467 | |
A | ASP489 | |
A | ASP491 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26306037, ECO:0000269|PubMed:35148176, ECO:0007744|PDB:4Y1T, ECO:0007744|PDB:7PAG |
Chain | Residue | Details |
A | ASP429 | |
A | ASN454 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:26306037, ECO:0000269|PubMed:35148176, ECO:0007744|PDB:3NSJ, ECO:0007744|PDB:4Y1T, ECO:0007744|PDB:7PAG |
Chain | Residue | Details |
A | ASP435 | |
A | ALA484 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:26306037, ECO:0007744|PDB:3NSJ, ECO:0007744|PDB:4Y1T |
Chain | Residue | Details |
A | ASP483 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:26306037, ECO:0007744|PDB:3NSJ, ECO:0007744|PDB:4Y1S |
Chain | Residue | Details |
A | ASP485 | |
A | ASP490 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21037563, ECO:0007744|PDB:3NSJ |
Chain | Residue | Details |
A | TRP488 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | SITE: Important for oligomerization => ECO:0000269|PubMed:19446473 |
Chain | Residue | Details |
A | GLU213 | |
A | GLU343 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:35148176, ECO:0007744|PDB:3NSJ, ECO:0007744|PDB:7PAG |
Chain | Residue | Details |
A | ASN204 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN375 | |
A | ASN548 |