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2ZCK

Crystal structure of a ternary complex between PSA, a substrat-acyl intermediate and an activating antibody

Functional Information from GO Data
ChainGOidnamespacecontents
L0002250biological_processadaptive immune response
L0002376biological_processimmune system process
L0005576cellular_componentextracellular region
L0005886cellular_componentplasma membrane
L0006955biological_processimmune response
L0019814cellular_componentimmunoglobulin complex
P0002803biological_processpositive regulation of antibacterial peptide production
P0003073biological_processregulation of systemic arterial blood pressure
P0004175molecular_functionendopeptidase activity
P0004252molecular_functionserine-type endopeptidase activity
P0005515molecular_functionprotein binding
P0005576cellular_componentextracellular region
P0005615cellular_componentextracellular space
P0005634cellular_componentnucleus
P0006508biological_processproteolysis
P0008233molecular_functionpeptidase activity
P0008236molecular_functionserine-type peptidase activity
P0016525biological_processnegative regulation of angiogenesis
P0016787molecular_functionhydrolase activity
P0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
P0030141cellular_componentsecretory granule
P0031638biological_processzymogen activation
P0032991cellular_componentprotein-containing complex
P0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
PLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. STcsGDSGGPLV
ChainResidueDetails
PSER189-VAL200

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
LTYR192-HIS198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues233
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"18187150","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
PASP102
PSER195
PHIS57

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
PASP102
PSER195
PHIS57
PGLY196

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
PASP102
PHIS57

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
PSER195
PGLY193

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
PSER195
PGLY196

site_idCSA6
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
PSER195
PGLY193
PASP95
PHIS57
PSER214

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
PSER195
PGLY193
PASP95
PHIS57

site_idCSA8
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
PASP102
PSER195
PGLY193
PHIS57

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PDB entries from 2025-12-03

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