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2OLG

Crystal structure of the serine protease domain of prophenoloxidase activating factor-I in a zymogen form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
AVAL151-CYS156

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScgGDSGGPLL
ChainResidueDetails
AASP309-LEU320

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues254
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":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17287215","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OLG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Cleavage","evidences":[{"source":"PubMed","id":"11012672","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9652393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9839951","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17287215","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2OLG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AHIS155
AASP220

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY316
ASER315

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AGLY313
ASER315

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AHIS155
ASER315
AASP220

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AHIS155
AGLY316
ASER315
AASP220

site_idCSA6
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AHIS155
AGLY313
ASER335
ASER315
AASP220

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
AHIS155
AGLY313
ASER315
AASP220

246704

PDB entries from 2025-12-24

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