1PQ8
Trypsin at pH 4 at atomic resolution
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 A 501 |
Chain | Residue |
A | ARG88 |
A | VAL183 |
A | SER184 |
A | SER185 |
A | HOH736 |
A | HOH831 |
A | HOH859 |
A | HOH890 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 502 |
Chain | Residue |
A | GLY112 |
A | GLY113 |
A | HOH672 |
A | HOH839 |
A | HOH913 |
A | GLN63 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 A 503 |
Chain | Residue |
A | GLY145 |
A | SER146 |
A | SER147 |
A | SER172 |
A | HOH678 |
A | HOH708 |
A | HOH809 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE LYS A 403 |
Chain | Residue |
A | SER190 |
A | CYS191 |
A | GLN192 |
A | GLY193 |
A | SER195 |
A | VAL210 |
A | SER211 |
A | GLY213 |
A | GLY215 |
C | GLY2 |
C | HOH4 |
C | HOH5 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE CIT A 601 |
Chain | Residue |
A | ALA22 |
A | SER23 |
A | ALA24 |
A | GLY25 |
A | ASP26 |
A | PHE27 |
A | PRO28 |
A | ILE30 |
A | GLY71 |
A | SER72 |
A | LEU73 |
A | ASN114 |
A | HOH750 |
A | HOH875 |
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 |