3V7T
Crystal Structure of Human Beta-Tryptase Complexed with a Synthetic Inhibitor with a Tropanylamide Scaffold
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 | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0062023 | cellular_component | collagen-containing extracellular matrix |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0062023 | cellular_component | collagen-containing extracellular matrix |
| 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 | 0008233 | molecular_function | peptidase activity |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0062023 | cellular_component | collagen-containing extracellular matrix |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005615 | cellular_component | extracellular space |
| D | 0006508 | biological_process | proteolysis |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0062023 | cellular_component | collagen-containing extracellular matrix |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 0GX A 301 |
| Chain | Residue |
| A | GLN102 |
| A | GLY232 |
| A | CO3302 |
| A | HOH427 |
| A | HOH454 |
| C | PRO63 |
| C | TYR99 |
| C | HOH434 |
| A | ASP203 |
| A | SER204 |
| A | CYS205 |
| A | GLN206 |
| A | SER209 |
| A | VAL227 |
| A | TRP229 |
| A | GLY230 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CO3 A 302 |
| Chain | Residue |
| A | PHE43 |
| A | HIS59 |
| A | GLN206 |
| A | GLY207 |
| A | SER209 |
| A | 0GX301 |
| A | HOH426 |
| A | HOH469 |
| A | HOH512 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 0GX B 301 |
| Chain | Residue |
| B | GLN102 |
| B | ASP203 |
| B | SER204 |
| B | CYS205 |
| B | GLN206 |
| B | SER209 |
| B | VAL227 |
| B | TRP229 |
| B | GLY230 |
| B | GLY232 |
| B | CO3302 |
| B | HOH415 |
| B | HOH462 |
| D | PRO63 |
| D | TYR99 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CO3 B 302 |
| Chain | Residue |
| B | PHE43 |
| B | HIS59 |
| B | GLN206 |
| B | GLY207 |
| B | SER209 |
| B | 0GX301 |
| B | HOH432 |
| B | HOH475 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 0GX C 301 |
| Chain | Residue |
| A | PRO63 |
| A | TYR99 |
| C | GLN102 |
| C | ASP203 |
| C | SER204 |
| C | CYS205 |
| C | GLN206 |
| C | SER209 |
| C | VAL227 |
| C | TRP229 |
| C | GLY230 |
| C | GLY232 |
| C | HOH417 |
| C | HOH460 |
| C | HOH469 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 0GX D 301 |
| Chain | Residue |
| B | PRO63 |
| B | TYR99 |
| D | GLN102 |
| D | ASP203 |
| D | SER204 |
| D | CYS205 |
| D | GLN206 |
| D | SER209 |
| D | VAL227 |
| D | TRP229 |
| D | GLY230 |
| D | GLY232 |
| D | CYS233 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU00274 |
| Chain | Residue | Details |
| A | HIS59 | |
| D | HIS59 | |
| D | ASP106 | |
| D | SER209 | |
| A | ASP106 | |
| A | SER209 | |
| B | HIS59 | |
| B | ASP106 | |
| B | SER209 | |
| C | HIS59 | |
| C | ASP106 | |
| C | SER209 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P21845 |
| Chain | Residue | Details |
| A | TYR82 | |
| B | TYR82 | |
| C | TYR82 | |
| D | TYR82 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN218 | |
| B | ASN218 | |
| C | ASN218 | |
| D | ASN218 |
