5WI6
Human beta-1 tryptase mutant Ile99Cys
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 | 0006952 | biological_process | defense response |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0022617 | biological_process | extracellular matrix disassembly |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0042802 | molecular_function | identical protein binding |
| 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 | 0006952 | biological_process | defense response |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0022617 | biological_process | extracellular matrix disassembly |
| B | 0031012 | cellular_component | extracellular matrix |
| B | 0042802 | molecular_function | identical protein binding |
| 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 | 0006952 | biological_process | defense response |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0022617 | biological_process | extracellular matrix disassembly |
| C | 0031012 | cellular_component | extracellular matrix |
| C | 0042802 | molecular_function | identical protein binding |
| 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 | 0006952 | biological_process | defense response |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0022617 | biological_process | extracellular matrix disassembly |
| D | 0031012 | cellular_component | extracellular matrix |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | ARG24 |
| A | GLN71 |
| A | TYR75 |
| A | GLN79 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue 0GJ A 302 |
| Chain | Residue |
| A | TRP215 |
| A | GLY216 |
| A | GLU217 |
| A | GLY219 |
| A | GLY226 |
| A | GLN98 |
| A | ASP189 |
| A | CYS191 |
| A | GLN192 |
| A | GLY193 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 301 |
| Chain | Residue |
| A | TYR75 |
| B | ARG24 |
| B | GLN71 |
| B | GLN79 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue 0GJ B 302 |
| Chain | Residue |
| B | GLN98 |
| B | ASP189 |
| B | CYS191 |
| B | GLN192 |
| B | GLY193 |
| B | TRP215 |
| B | GLY216 |
| B | GLU217 |
| B | GLY219 |
| B | GLY226 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 301 |
| Chain | Residue |
| C | LYS26 |
| C | LYS202 |
| C | TRP207 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 302 |
| Chain | Residue |
| C | ARG24 |
| C | GLN71 |
| C | TYR75 |
| C | GLN79 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue 0GJ C 303 |
| Chain | Residue |
| C | GLN98 |
| C | ASP189 |
| C | CYS191 |
| C | GLN192 |
| C | GLY193 |
| C | TRP215 |
| C | GLY216 |
| C | GLY219 |
| C | GLY226 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 301 |
| Chain | Residue |
| D | GLY19 |
| D | GLN20 |
| D | TRP137 |
| D | GLN157 |
| D | VAL158 |
| D | LYS159 |
| D | ARG188 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 302 |
| Chain | Residue |
| C | TYR75 |
| D | ARG24 |
| D | GLU70 |
| D | GLN71 |
| D | GLN79 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 D 303 |
| Chain | Residue |
| D | LYS202 |
| D | TRP207 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue 0GJ D 304 |
| Chain | Residue |
| D | GLN98 |
| D | ASP189 |
| D | CYS191 |
| D | GLN192 |
| D | GLY193 |
| D | TRP215 |
| D | GLY216 |
| D | GLY219 |
| D | GLY226 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 964 |
| 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 | 12 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






