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3I74

Crystal Structure of the plant subtilisin-like protease SBT3 in complex with a chloromethylketone inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
Functional Information from PROSITE/UniProt
site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAaPhAAG
ChainResidueDetails
AGLY536-GLY546

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP144
BASP144

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:19805099
ChainResidueDetails
AHIS215
BHIS215

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240, ECO:0000269|PubMed:19332543, ECO:0000269|PubMed:19805099
ChainResidueDetails
ASER538
BSER538

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) (paucimannose) asparagine; alternate => ECO:0000269|PubMed:19332543
ChainResidueDetails
AASN177
AASN203
AASN697
AASN745
BASN177
BASN203
BASN697
BASN745

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (paucimannose) asparagine; partial => ECO:0000269|PubMed:19332543
ChainResidueDetails
AASN376
BASN376

220113

PDB entries from 2024-05-22

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