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4WVP

Crystal structure of an activity-based probe HNE complex

Functional Information from GO Data
ChainGOidnamespacecontents
E0000122biological_processnegative regulation of transcription by RNA polymerase II
E0001878biological_processresponse to yeast
E0002020molecular_functionprotease binding
E0002438biological_processacute inflammatory response to antigenic stimulus
E0002523biological_processleukocyte migration involved in inflammatory response
E0002812biological_processbiosynthetic process of antibacterial peptides active against Gram-negative bacteria
E0003714molecular_functiontranscription corepressor activity
E0004175molecular_functionendopeptidase activity
E0004252molecular_functionserine-type endopeptidase activity
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005615cellular_componentextracellular space
E0005737cellular_componentcytoplasm
E0005794cellular_componentGolgi apparatus
E0005829cellular_componentcytosol
E0006508biological_processproteolysis
E0006874biological_processintracellular calcium ion homeostasis
E0006909biological_processphagocytosis
E0008201molecular_functionheparin binding
E0008233molecular_functionpeptidase activity
E0008236molecular_functionserine-type peptidase activity
E0009411biological_processresponse to UV
E0009986cellular_componentcell surface
E0016787molecular_functionhydrolase activity
E0017053cellular_componenttranscription repressor complex
E0019955molecular_functioncytokine binding
E0022617biological_processextracellular matrix disassembly
E0030141cellular_componentsecretory granule
E0030163biological_processprotein catabolic process
E0031012cellular_componentextracellular matrix
E0031410cellular_componentcytoplasmic vesicle
E0032496biological_processresponse to lipopolysaccharide
E0032682biological_processnegative regulation of chemokine production
E0032717biological_processnegative regulation of interleukin-8 production
E0032757biological_processpositive regulation of interleukin-8 production
E0035578cellular_componentazurophil granule lumen
E0035580cellular_componentspecific granule lumen
E0042742biological_processdefense response to bacterium
E0043406biological_processpositive regulation of MAP kinase activity
E0045335cellular_componentphagocytic vesicle
E0048661biological_processpositive regulation of smooth muscle cell proliferation
E0050728biological_processnegative regulation of inflammatory response
E0050778biological_processpositive regulation of immune response
E0050832biological_processdefense response to fungus
E0050900biological_processleukocyte migration
E0050922biological_processnegative regulation of chemotaxis
E0070062cellular_componentextracellular exosome
E0070269biological_processpyroptotic inflammatory response
E0070945biological_processneutrophil-mediated killing of gram-negative bacterium
E0070947biological_processneutrophil-mediated killing of fungus
E1903238biological_processpositive regulation of leukocyte tethering or rolling
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. MSAAHC
ChainResidueDetails
EMET53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. GVcfGDSGSPLV
ChainResidueDetails
EGLY189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues217
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":"2911584","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"26274980","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3550808","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3550808","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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