Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3NSJ

The X-ray crystal structure of lymphocyte perforin

Functional Information from GO Data
ChainGOidnamespacecontents
A0001771biological_processimmunological synapse formation
A0001772cellular_componentimmunological synapse
A0001909biological_processleukocyte mediated cytotoxicity
A0001913biological_processT cell mediated cytotoxicity
A0002357biological_processdefense response to tumor cell
A0002418biological_processimmune response to tumor cell
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0005768cellular_componentendosome
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0007623biological_processcircadian rhythm
A0009306biological_processprotein secretion
A0016020cellular_componentmembrane
A0017038biological_processprotein import
A0022829molecular_functionwide pore channel activity
A0031410cellular_componentcytoplasmic vesicle
A0031640biological_processkilling of cells of another organism
A0031904cellular_componentendosome lumen
A0042802molecular_functionidentical protein binding
A0044194cellular_componentcytolytic granule
A0046872molecular_functionmetal ion binding
A0051260biological_processprotein homooligomerization
A0051607biological_processdefense response to virus
A0051712biological_processpositive regulation of killing of cells of another organism
A0071806biological_processprotein transmembrane transport
A0140507biological_processgranzyme-mediated programmed cell death signaling pathway
A0140911molecular_functionpore-forming activity
Functional Information from PROSITE/UniProt
site_idPS00279
Number of Residues12
DetailsMACPF_1 Membrane attack complex/perforin (MACPF) domain signature. YhelissYGTHF
ChainResidueDetails
ATYR211-PHE222

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTRANSMEM: Beta stranded; Name=CH1 => ECO:0000305|PubMed:21037563
ChainResidueDetails
ATRP128-GLY148

site_idSWS_FT_FI2
Number of Residues22
DetailsTRANSMEM: Beta stranded; Name=CH2 => ECO:0000305|PubMed:21037563
ChainResidueDetails
ACYS256-CYS278

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:26306037, ECO:0007744|PDB:4Y1T
ChainResidueDetails
AGLY428
ATHR432
AALA433
AGLU467
AASP489
AASP491

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:26306037, ECO:0000269|PubMed:35148176, ECO:0007744|PDB:4Y1T, ECO:0007744|PDB:7PAG
ChainResidueDetails
AASP429
AASN454

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: 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
ChainResidueDetails
AASP435
AALA484

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:26306037, ECO:0007744|PDB:3NSJ, ECO:0007744|PDB:4Y1T
ChainResidueDetails
AASP483

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:26306037, ECO:0007744|PDB:3NSJ, ECO:0007744|PDB:4Y1S
ChainResidueDetails
AASP485
AASP490

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21037563, ECO:0007744|PDB:3NSJ
ChainResidueDetails
ATRP488

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Important for oligomerization => ECO:0000269|PubMed:19446473
ChainResidueDetails
AGLU213
AGLU343

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21037563, ECO:0000269|PubMed:35148176, ECO:0007744|PDB:3NSJ, ECO:0007744|PDB:7PAG
ChainResidueDetails
AASN204

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN375
AASN548

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon