2G51
anomalous substructure of trypsin (p1)
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 | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 240 |
| Chain | Residue |
| A | SER74 |
| A | HIS90 |
| A | VAL150 |
| A | PHE234 |
| A | HOH295 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 241 |
| Chain | Residue |
| A | SER184 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 242 |
| Chain | Residue |
| A | GLY113 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 223 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Required for specificity"} |
| Chain | Residue | Details |
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 | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | HIS56 | |
| A | ASP99 |
| site_id | CSA4 |
| 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 | CSA5 |
| 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 | CSA6 |
| 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 | 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 |
