4MPW
Human beta-tryptase co-crystal structure with [(1,1,3,3-tetramethyldisiloxane-1,3-diyl)di-1-benzofuran-3,5-diyl]bis({4-[3-(aminomethyl)phenyl]piperidin-1-yl}methanone)
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 | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0022617 | biological_process | extracellular matrix disassembly |
| A | 0042802 | molecular_function | identical protein binding |
| 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 | 0006952 | biological_process | defense response |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0022617 | biological_process | extracellular matrix disassembly |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0062023 | cellular_component | collagen-containing extracellular matrix |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 301 |
| Chain | Residue |
| A | TRP42 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PGE A 302 |
| Chain | Residue |
| A | VAL50 |
| A | PHE58 |
| A | LYS81 |
| A | ASP82 |
| A | ALA85 |
| A | HOH614 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 303 |
| Chain | Residue |
| A | GLN221 |
| A | GLY222 |
| A | SER224 |
| A | HOH466 |
| A | HOH554 |
| A | PHE58 |
| A | HIS74 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE 2AJ B 301 |
| Chain | Residue |
| A | THR115 |
| A | GLN117 |
| A | ASP218 |
| A | SER219 |
| A | CYS220 |
| A | GLN221 |
| A | SER224 |
| A | TRP244 |
| A | GLY245 |
| A | GLU246 |
| A | GLY247 |
| B | THR115 |
| B | GLN117 |
| B | ASP218 |
| B | SER219 |
| B | CYS220 |
| B | GLN221 |
| B | SER224 |
| B | TRP244 |
| B | GLY245 |
| B | GLU246 |
| B | GLY247 |
| B | HOH410 |
| B | HOH426 |
| B | HOH438 |
| B | HOH519 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT B 302 |
| Chain | Residue |
| B | PHE58 |
| B | HIS74 |
| B | GLN221 |
| B | GLY222 |
| B | SER224 |
| B | HOH414 |
| B | HOH464 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 303 |
| Chain | Residue |
| B | TRP42 |
| B | TRP44 |
| B | HOH557 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE B 304 |
| Chain | Residue |
| B | PHE58 |
| B | LYS81 |
| B | ASP82 |
| B | HOH463 |
| B | HOH593 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| A | HIS74 | |
| A | ASP121 | |
| A | SER224 | |
| B | HIS74 | |
| B | ASP121 | |
| B | SER224 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | LYS132 | |
| B | LYS132 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218 |
| Chain | Residue | Details |
| A | ASN233 | |
| B | ASN233 |
