1PQ7
Trypsin at 0.8 A, pH5 / borax
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008236 | molecular_function | serine-type peptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 601 |
Chain | Residue |
A | ARG119 |
A | ASN220 |
A | ARG232 |
A | HOH781 |
A | HOH831 |
A | HOH891 |
A | HOH977 |
A | HOH1079 |
A | HOH1086 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 602 |
Chain | Residue |
A | ARG88 |
A | SER184 |
A | SER185 |
A | HOH839 |
A | HOH870 |
A | HOH895 |
A | HOH917 |
A | HOH966 |
A | HOH1045 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE ARG A 703 |
Chain | Residue |
A | HIS56 |
A | ASP189 |
A | SER190 |
A | CYS191 |
A | GLN192 |
A | GLY193 |
A | SER195 |
A | VAL210 |
A | SER211 |
A | TRP212 |
A | GLY213 |
A | GLY215 |
A | GLY223 |
A | HOH704 |
A | HOH705 |
A | HOH901 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | ACT_SITE: Charge relay system |
Chain | Residue | Details |
A | HIS56 | |
A | ASP99 | |
A | SER195 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Required for specificity |
Chain | Residue | Details |
A | ASP189 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | HIS56 | |
A | ASP99 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER195 | |
A | GLY196 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER195 | |
A | GLY193 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER195 | |
A | HIS56 | |
A | ASP99 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER195 | |
A | GLY193 | |
A | HIS56 | |
A | ASP99 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER195 | |
A | HIS56 | |
A | ASP99 | |
A | GLY196 |
site_id | CSA7 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | SER195 | |
A | SER211 | |
A | GLY193 | |
A | HIS56 | |
A | ASP99 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 173 |
Chain | Residue | Details |
A | HIS56 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ASP99 | activator, electrostatic stabiliser, hydrogen bond acceptor |
A | GLN192 | electrostatic stabiliser, hydrogen bond donor, transition state stabiliser |
A | GLY193 | electrostatic stabiliser, hydrogen bond donor, transition state stabiliser |
A | ASP194 | electrostatic stabiliser, hydrogen bond donor, transition state stabiliser |
A | SER195 | electrostatic stabiliser, transition state stabiliser |