4A6L
beta-tryptase inhibitor
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 | 16 |
Details | BINDING SITE FOR RESIDUE P43 A 1263 |
Chain | Residue |
A | GLN105 |
A | TRP233 |
A | GLY234 |
A | GLU235 |
A | GLY237 |
A | HOH2053 |
C | ASP64 |
C | TYR102 |
A | TYR181 |
A | ILE193 |
A | ASP207 |
A | SER208 |
A | CYS209 |
A | GLN210 |
A | SER213 |
A | VAL231 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE P43 B 1263 |
Chain | Residue |
B | GLN105 |
B | TYR181 |
B | ILE193 |
B | ASP207 |
B | SER208 |
B | CYS209 |
B | SER213 |
B | VAL231 |
B | TRP233 |
B | GLY234 |
B | GLU235 |
B | GLY237 |
B | HOH2086 |
D | ASP64 |
D | TYR102 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE P43 C 1263 |
Chain | Residue |
A | ASP64 |
A | TYR102 |
C | GLN105 |
C | TYR181 |
C | ILE193 |
C | ASP207 |
C | SER208 |
C | CYS209 |
C | GLN210 |
C | SER213 |
C | VAL231 |
C | TRP233 |
C | GLY234 |
C | GLU235 |
C | GLY237 |
C | ARG243 |
C | GLY245 |
C | HOH2080 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE P43 D 1263 |
Chain | Residue |
B | ASP64 |
B | TYR102 |
D | GLN105 |
D | TYR181 |
D | ILE193 |
D | ASP207 |
D | SER208 |
D | SER213 |
D | VAL231 |
D | TRP233 |
D | GLY234 |
D | GLU235 |
D | GLY237 |
D | GLY245 |
D | HOH2077 |
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 | ASP109 | |
D | SER213 | |
A | ASP109 | |
A | SER213 | |
B | HIS59 | |
B | ASP109 | |
B | SER213 | |
C | HIS59 | |
C | ASP109 | |
C | SER213 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | LYS120 | |
A | ASN222 | |
B | LYS120 | |
B | ASN222 | |
C | LYS120 | |
C | ASN222 | |
D | LYS120 | |
D | ASN222 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P21845 |
Chain | Residue | Details |
A | TYR82 | |
B | TYR82 | |
C | TYR82 | |
D | TYR82 |