1EJM
CRYSTAL STRUCTURE OF THE BPTI ALA16LEU MUTANT IN COMPLEX WITH BOVINE TRYPSIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004175 | molecular_function | endopeptidase activity |
| 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 | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097180 | cellular_component | serine protease inhibitor complex |
| A | 0097655 | molecular_function | serpin family protein binding |
| B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| C | 0004175 | molecular_function | endopeptidase 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 | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0097180 | cellular_component | serine protease inhibitor complex |
| C | 0097655 | molecular_function | serpin family protein binding |
| D | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| E | 0004175 | molecular_function | endopeptidase 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 | 0008236 | molecular_function | serine-type peptidase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0097180 | cellular_component | serine protease inhibitor complex |
| E | 0097655 | molecular_function | serpin family protein binding |
| F | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3601 |
| Chain | Residue |
| C | LYS60 |
| C | HOH4359 |
| D | ARG520 |
| D | LYS546 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 F 3602 |
| Chain | Residue |
| D | ARG542 |
| F | ARG520 |
| F | TYR535 |
| F | HOH4284 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3603 |
| Chain | Residue |
| B | LYS541 |
| B | ARG542 |
| B | HOH4120 |
| B | HOH4539 |
| B | HOH4565 |
| B | GLU507 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3604 |
| Chain | Residue |
| D | ARG520 |
| D | TYR535 |
| D | HOH4142 |
| F | ARG542 |
| F | HOH4399 |
| F | HOH4538 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 F 3605 |
| Chain | Residue |
| D | LYS541 |
| D | SO43606 |
| D | HOH4134 |
| F | TYR510 |
| F | ARG539 |
| F | HOH4117 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3606 |
| Chain | Residue |
| D | TYR510 |
| D | ARG539 |
| F | TYR510 |
| F | SO43605 |
| F | HOH4298 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3607 |
| Chain | Residue |
| B | ARG520 |
| B | TYR535 |
| B | GLY537 |
| B | ALA540 |
| B | HOH4023 |
| B | HOH4500 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 E 3608 |
| Chain | Residue |
| E | ASN100 |
| E | ASN101 |
| E | ASN179 |
| E | HOH4355 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 3609 |
| Chain | Residue |
| A | LYS60 |
| B | ILE519 |
| B | ARG520 |
| B | LYS546 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3610 |
| Chain | Residue |
| A | ASN100 |
| A | ASN101 |
| A | ASN179 |
| A | HOH4203 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 3611 |
| Chain | Residue |
| D | PRO509 |
| D | TYR510 |
| D | THR511 |
| D | GLY512 |
| D | HOH4469 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 C 3612 |
| Chain | Residue |
| C | LYS169 |
| C | PRO173 |
| C | GLY174 |
| C | HOH4048 |
| C | HOH4510 |
| C | HOH4576 |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC |
| Chain | Residue | Details |
| A | VAL53-CYS58 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPVV |
| Chain | Residue | Details |
| A | ASP189-VAL200 |
| site_id | PS00280 |
| Number of Residues | 19 |
| Details | BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGCrakrnnFksaedC |
| Chain | Residue | Details |
| B | PHE533-CYS551 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | SITE: Reactive bond for trypsin |
| Chain | Residue | Details |
| B | ARG515 | |
| D | ARG515 | |
| F | ARG515 | |
| C | LYS60 | |
| C | LEU105 | |
| C | PRO198 | |
| E | LYS60 | |
| E | LEU105 | |
| E | PRO198 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 21 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ILE73 | |
| C | GLY78 | |
| C | ILE83 | |
| C | GLN192 | |
| C | SER195 | |
| C | PRO198 | |
| E | ILE73 | |
| E | VAL75 | |
| E | GLY78 | |
| E | ILE83 | |
| E | GLN192 | |
| A | VAL75 | |
| E | SER195 | |
| E | PRO198 | |
| A | GLY78 | |
| A | ILE83 | |
| A | GLN192 | |
| A | SER195 | |
| A | PRO198 | |
| C | ILE73 | |
| C | VAL75 |
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 |
| C | ASP102 | |
| C | SER195 | |
| C | HIS57 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | ASP102 | |
| E | SER195 | |
| E | HIS57 |
| site_id | CSA4 |
| 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 | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | ASP102 | |
| C | SER195 | |
| C | GLY193 | |
| C | HIS57 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | ASP102 | |
| E | SER195 | |
| E | GLY193 | |
| E | 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 |
| C | ASP102 | |
| C | SER195 | |
| C | HIS57 | |
| C | GLY196 |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| E | ASP102 | |
| E | SER195 | |
| E | HIS57 | |
| E | GLY196 |
