4MPU
Human beta-tryptase co-crystal structure with (6S,8R)-N,N'-bis[3-({4-[3-(aminomethyl)phenyl]piperidin-1-yl}carbonyl)phenyl]-8-hydroxy-6-(1-hydroxycyclobutyl)-5,7-dioxaspiro[3.4]octane-6,8-dicarboxamide
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 | 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 | 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 | 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 | 15 |
| Details | BINDING SITE FOR RESIDUE MES A 301 |
| Chain | Residue |
| A | PRO103 |
| A | HOH431 |
| A | HOH471 |
| A | HOH507 |
| A | HOH521 |
| A | HOH637 |
| A | HOH646 |
| A | GLN112 |
| A | ILE118 |
| A | GLY119 |
| A | ASP207 |
| A | ASP208 |
| A | TYR262 |
| A | TYR263 |
| A | HOH430 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | HIS74 |
| A | GLN221 |
| A | GLY222 |
| A | SER224 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PG4 A 303 |
| Chain | Residue |
| A | VAL50 |
| A | PHE58 |
| A | VAL80 |
| A | LYS81 |
| A | ASP82 |
| A | ALA85 |
| A | HOH517 |
| A | HOH525 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE X2A 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 |
| A | HOH424 |
| A | HOH532 |
| B | GLN117 |
| B | ASP218 |
| B | SER219 |
| B | CYS220 |
| B | SER224 |
| B | TRP244 |
| B | GLY245 |
| B | GLU246 |
| B | GLY247 |
| B | HOH432 |
| B | HOH513 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MES B 302 |
| Chain | Residue |
| A | LYS132 |
| A | SER134 |
| A | HIS136 |
| A | HOH417 |
| B | ARG203 |
| B | ARG206 |
| B | ASP207 |
| B | SO4305 |
| B | HOH474 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 303 |
| Chain | Residue |
| B | ASN214 |
| B | THR215 |
| B | ARG216 |
| B | HOH556 |
| B | HOH624 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 304 |
| Chain | Residue |
| B | HIS74 |
| B | GLN221 |
| B | GLY222 |
| B | SER224 |
| B | HOH555 |
| B | HOH604 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 305 |
| Chain | Residue |
| A | HIS136 |
| B | HIS186 |
| B | ARG203 |
| B | MES302 |
| B | HOH426 |
| B | HOH537 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 B 306 |
| Chain | Residue |
| B | VAL50 |
| B | LYS81 |
| B | ASP82 |
| B | ALA85 |
| B | HOH484 |
| B | HOH572 |
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 |
