2FPZ
Human tryptase with 2-amino benzimidazole
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 | 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 | 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 | 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 | 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 | 9 |
Details | BINDING SITE FOR RESIDUE 270 A 1000 |
Chain | Residue |
A | ASP189 |
A | SER190 |
A | CYS191 |
A | GLN192 |
A | SER195 |
A | GLY216 |
A | GLY219 |
A | GLY226 |
A | HOH1093 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 270 B 1001 |
Chain | Residue |
B | ASP189 |
B | SER190 |
B | CYS191 |
B | GLN192 |
B | SER195 |
B | GLY216 |
B | GLY219 |
B | GLY226 |
B | HOH1039 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 270 C 1002 |
Chain | Residue |
C | ASP189 |
C | SER190 |
C | CYS191 |
C | GLN192 |
C | SER195 |
C | GLY216 |
C | GLY219 |
C | GLY226 |
C | HOH1090 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 270 D 1003 |
Chain | Residue |
D | ASP189 |
D | SER190 |
D | CYS191 |
D | SER195 |
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 | 12 |
Details | ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU00274 |
Chain | Residue | Details |
A | HIS57 | |
D | HIS57 | |
D | ASP102 | |
D | SER195 | |
A | ASP102 | |
A | SER195 | |
B | HIS57 | |
B | ASP102 | |
B | SER195 | |
C | HIS57 | |
C | ASP102 | |
C | SER195 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P21845 |
Chain | Residue | Details |
A | TYR75 | |
B | TYR75 | |
C | TYR75 | |
D | TYR75 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN204 | |
B | ASN204 | |
C | ASN204 | |
D | ASN204 |
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 | CSA10 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
B | ASP102 | |
B | SER195 | |
B | HIS57 | |
B | GLY196 |
site_id | CSA11 |
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 | CSA12 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
D | ASP102 | |
D | SER195 | |
D | HIS57 | |
D | GLY196 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
B | ASP102 | |
B | SER195 | |
B | HIS57 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
C | ASP102 | |
C | SER195 | |
C | HIS57 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
D | ASP102 | |
D | SER195 | |
D | HIS57 |
site_id | CSA5 |
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 | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
B | ASP102 | |
B | SER195 | |
B | GLY193 | |
B | HIS57 |
site_id | CSA7 |
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 | CSA8 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
D | ASP102 | |
D | SER195 | |
D | GLY193 | |
D | HIS57 |
site_id | CSA9 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
A | ASP102 | |
A | SER195 | |
A | HIS57 | |
A | GLY196 |