Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005615 | cellular_component | extracellular space |
A | 0006508 | biological_process | proteolysis |
A | 0006952 | biological_process | defense response |
A | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0022617 | biological_process | extracellular matrix disassembly |
A | 0031012 | cellular_component | extracellular matrix |
A | 0042802 | molecular_function | identical protein binding |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0006508 | biological_process | proteolysis |
B | 0006952 | biological_process | defense response |
B | 0008233 | molecular_function | peptidase activity |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0022617 | biological_process | extracellular matrix disassembly |
B | 0031012 | cellular_component | extracellular matrix |
B | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE MES A 301 |
Chain | Residue |
A | PRO103 |
A | HOH431 |
A | HOH471 |
A | HOH507 |
A | HOH521 |
A | HOH637 |
A | HOH646 |
A | GLN112 |
A | ILE118 |
A | GLY119 |
A | ASP207 |
A | ASP208 |
A | TYR262 |
A | TYR263 |
A | HOH430 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | HIS74 |
A | GLN221 |
A | GLY222 |
A | SER224 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PG4 A 303 |
Chain | Residue |
A | VAL50 |
A | PHE58 |
A | VAL80 |
A | LYS81 |
A | ASP82 |
A | ALA85 |
A | HOH517 |
A | HOH525 |
site_id | AC4 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE X2A B 301 |
Chain | Residue |
A | THR115 |
A | GLN117 |
A | ASP218 |
A | SER219 |
A | CYS220 |
A | GLN221 |
A | SER224 |
A | TRP244 |
A | GLY245 |
A | GLU246 |
A | GLY247 |
A | HOH424 |
A | HOH532 |
B | GLN117 |
B | ASP218 |
B | SER219 |
B | CYS220 |
B | SER224 |
B | TRP244 |
B | GLY245 |
B | GLU246 |
B | GLY247 |
B | HOH432 |
B | HOH513 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MES B 302 |
Chain | Residue |
A | LYS132 |
A | SER134 |
A | HIS136 |
A | HOH417 |
B | ARG203 |
B | ARG206 |
B | ASP207 |
B | SO4305 |
B | HOH474 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 303 |
Chain | Residue |
B | ASN214 |
B | THR215 |
B | ARG216 |
B | HOH556 |
B | HOH624 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 304 |
Chain | Residue |
B | HIS74 |
B | GLN221 |
B | GLY222 |
B | SER224 |
B | HOH555 |
B | HOH604 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 305 |
Chain | Residue |
A | HIS136 |
B | HIS186 |
B | ARG203 |
B | MES302 |
B | HOH426 |
B | HOH537 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG4 B 306 |
Chain | Residue |
B | VAL50 |
B | LYS81 |
B | ASP82 |
B | ALA85 |
B | HOH484 |
B | HOH572 |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
Chain | Residue | Details |
A | LEU70-CYS75 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV |
Chain | Residue | Details |
A | ASP218-VAL229 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 482 |
Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Active site: {"description":"Charge relay system"} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |