4DOQ
Crystal structure of the complex of Porcine Pancreatic Trypsin with 1/2SLPI
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 | 0007586 | biological_process | digestion |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005615 | cellular_component | extracellular space |
| C | 0006508 | biological_process | proteolysis |
| C | 0007586 | biological_process | digestion |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0030414 | molecular_function | peptidase inhibitor activity |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005576 | cellular_component | extracellular region |
| E | 0005615 | cellular_component | extracellular space |
| E | 0006508 | biological_process | proteolysis |
| E | 0007586 | biological_process | digestion |
| E | 0008233 | molecular_function | peptidase activity |
| E | 0008236 | molecular_function | serine-type peptidase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE XPE A 301 |
| Chain | Residue |
| A | ALA56 |
| B | CYS97 |
| B | SER100 |
| A | HIS57 |
| A | TYR59 |
| A | THR90 |
| A | PHE94 |
| A | GLY96 |
| A | HOH454 |
| A | HOH455 |
| B | PHE79 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | PHE41 |
| A | LYS60 |
| A | HOH480 |
| B | ASN75 |
| B | HOH309 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | ALA130 |
| A | ALA132 |
| A | HOH479 |
| A | HOH492 |
| C | ALA130 |
| C | ALA132 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 304 |
| Chain | Residue |
| A | GLU70 |
| A | ASN72 |
| A | VAL75 |
| A | GLU77 |
| A | GLU80 |
| A | HOH429 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 B 201 |
| Chain | Residue |
| B | TYR68 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE P6G C 301 |
| Chain | Residue |
| C | ALA56 |
| C | PHE94 |
| C | GLY96 |
| C | HOH471 |
| D | PHE79 |
| D | CYS97 |
| D | SER100 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 C 302 |
| Chain | Residue |
| C | TYR20 |
| C | THR21 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 303 |
| Chain | Residue |
| C | GLU70 |
| C | ASN72 |
| C | VAL75 |
| C | GLU77 |
| C | GLU80 |
| C | HOH441 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 201 |
| Chain | Residue |
| D | LYS60 |
| D | PRO61 |
| D | HOH331 |
| D | HOH338 |
| E | ARG66 |
| E | HOH429 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 202 |
| Chain | Residue |
| C | GLN175 |
| D | VAL66 |
| D | THR67 |
| D | TYR68 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 E 301 |
| Chain | Residue |
| C | ARG62 |
| E | TYR20 |
| E | THR21 |
| E | HOH434 |
| E | HOH468 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA E 302 |
| Chain | Residue |
| E | GLU69 |
| E | ASN71 |
| E | VAL74 |
| E | GLU76 |
| E | GLU79 |
| E | HOH449 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Site: {"description":"Required for specificity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Reactive bond for chymotrypsin, trypsin and elastase","evidences":[{"source":"PubMed","id":"18421166","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24121345","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"3366116","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
