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1FQ3

CRYSTAL STRUCTURE OF HUMAN GRANZYME B

Functional Information from GO Data
ChainGOidnamespacecontents
A0001772cellular_componentimmunological synapse
A0001778biological_processplasma membrane repair
A0002839biological_processpositive regulation of immune response to tumor cell
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0009306biological_processprotein secretion
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0017148biological_processnegative regulation of translation
A0031640biological_processkilling of cells of another organism
A0042267biological_processnatural killer cell mediated cytotoxicity
A0044194cellular_componentcytolytic granule
A0046513biological_processceramide biosynthetic process
A0051603biological_processproteolysis involved in protein catabolic process
A0051604biological_processprotein maturation
A0070269biological_processpyroptotic inflammatory response
A0140507biological_processgranzyme-mediated programmed cell death signaling pathway
A0141201biological_processpyroptotic cell death
A1903749biological_processpositive regulation of establishment of protein localization to mitochondrion
A1904856cellular_componentcytolytic granule lumen
B0001772cellular_componentimmunological synapse
B0001778biological_processplasma membrane repair
B0002839biological_processpositive regulation of immune response to tumor cell
B0004252molecular_functionserine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0006915biological_processapoptotic process
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0009306biological_processprotein secretion
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0017148biological_processnegative regulation of translation
B0031640biological_processkilling of cells of another organism
B0042267biological_processnatural killer cell mediated cytotoxicity
B0044194cellular_componentcytolytic granule
B0046513biological_processceramide biosynthetic process
B0051603biological_processproteolysis involved in protein catabolic process
B0051604biological_processprotein maturation
B0070269biological_processpyroptotic inflammatory response
B0140507biological_processgranzyme-mediated programmed cell death signaling pathway
B0141201biological_processpyroptotic cell death
B1903749biological_processpositive regulation of establishment of protein localization to mitochondrion
B1904856cellular_componentcytolytic granule lumen
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ALEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. TSfkGDSGGPLV
ChainResidueDetails
ATHR189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues448
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"11209755","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11325591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Mediates preference for Asp-containing substrates","evidences":[{"source":"UniProtKB","id":"P18291","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11325591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BGLY193
BHIS57

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AASP102
ASER195
AHIS57
AGLY196

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
BASP102
BSER195
BHIS57
BGLY196

239149

PDB entries from 2025-07-23

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