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 | 0006508 | biological_process | proteolysis |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0022617 | biological_process | extracellular matrix disassembly |
A | 0030141 | cellular_component | secretory granule |
A | 0031214 | biological_process | biomineral tissue development |
A | 0046872 | molecular_function | metal ion binding |
A | 0097186 | biological_process | amelogenesis |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005576 | cellular_component | extracellular region |
B | 0006508 | biological_process | proteolysis |
B | 0008236 | molecular_function | serine-type peptidase activity |
B | 0022617 | biological_process | extracellular matrix disassembly |
B | 0030141 | cellular_component | secretory granule |
B | 0031214 | biological_process | biomineral tissue development |
B | 0046872 | molecular_function | metal ion binding |
B | 0097186 | biological_process | amelogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 401 |
Chain | Residue |
A | LEU99 |
A | ASP102 |
A | MET180 |
A | SER214 |
A | HOH412 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 402 |
Chain | Residue |
A | CYS232 |
A | PRO129 |
A | GLN210 |
A | ASN230 |
A | LEU231 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CL B 403 |
Chain | Residue |
B | LEU98 |
B | SER164 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 404 |
Chain | Residue |
A | LEU98 |
A | VAL163 |
A | SER164 |
A | VAL167 |
A | HOH498 |
A | HOH529 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE NI A 405 |
Chain | Residue |
A | HIS25 |
A | GLU77 |
A | HOH480 |
A | HOH483 |
A | HOH486 |
A | HOH557 |
A | HOH563 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NI B 406 |
Chain | Residue |
B | HIS25 |
B | GLU77 |
B | HOH534 |
B | HOH535 |
B | HOH536 |
B | HOH537 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NI B 407 |
Chain | Residue |
B | THR64 |
B | HOH538 |
B | HOH539 |
B | HOH540 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NI A 408 |
Chain | Residue |
A | ASN37 |
A | HOH531 |
A | HOH550 |
A | HOH556 |
A | HOH558 |
A | HOH560 |
site_id | AC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PBZ A 301 |
Chain | Residue |
A | ASP189 |
A | SER190 |
A | ASN192 |
A | SER195 |
A | VAL213 |
A | PHE215 |
A | CYS220 |
A | GLY226 |
A | HOH424 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PBZ B 302 |
Chain | Residue |
B | ASP189 |
B | SER190 |
B | SER195 |
B | VAL213 |
B | PHE215 |
B | GLY216 |
B | LYS217 |
B | CYS220 |
B | GLY226 |
B | HOH415 |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LSAAHC |
Chain | Residue | Details |
A | LEU53-CYS58 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScnGDSGGPLI |
Chain | Residue | Details |
A | ASP189-ILE200 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS57 | |
A | ASP102 | |
A | SER195 | |
B | HIS57 | |
B | ASP102 | |
B | SER195 | |
Chain | Residue | Details |
A | HIS25 | |
A | GLU77 | |
B | HIS25 | |
B | GLU77 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN159 | |
B | ASN159 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | ASP102 | |
A | SER195 | |
A | HIS57 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
B | ASP102 | |
B | SER195 | |
B | HIS57 | |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER195 | |
A | ALA100 | |
A | HIS57 | |
A | GLY196 | |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
B | SER195 | |
B | ALA100 | |
B | HIS57 | |
B | GLY196 | |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | ASP102 | |
A | SER195 | |
A | GLY193 | |
A | HIS57 | |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
B | ASP102 | |
B | SER195 | |
B | GLY193 | |
B | HIS57 | |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | ASP102 | |
A | SER195 | |
A | HIS57 | |
A | GLY196 | |
site_id | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
B | ASP102 | |
B | SER195 | |
B | HIS57 | |
B | GLY196 | |