6NVB
Crystal structure of the inhibitor-free form of the serine protease kallikrein-4
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 | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0022617 | biological_process | extracellular matrix disassembly |
| A | 0030141 | cellular_component | secretory granule |
| A | 0031214 | biological_process | biomineral tissue development |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097186 | biological_process | amelogenesis |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0022617 | biological_process | extracellular matrix disassembly |
| B | 0030141 | cellular_component | secretory granule |
| B | 0031214 | biological_process | biomineral tissue development |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0097186 | biological_process | amelogenesis |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0006508 | biological_process | proteolysis |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0022617 | biological_process | extracellular matrix disassembly |
| C | 0030141 | cellular_component | secretory granule |
| C | 0031214 | biological_process | biomineral tissue development |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0097186 | biological_process | amelogenesis |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0006508 | biological_process | proteolysis |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0022617 | biological_process | extracellular matrix disassembly |
| D | 0030141 | cellular_component | secretory granule |
| D | 0031214 | biological_process | biomineral tissue development |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0097186 | biological_process | amelogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | ASP189 |
| A | GLY226 |
| A | HOH427 |
| A | HOH473 |
| A | SER190 |
| A | LYS217 |
| A | PRO219 |
| A | CYS220 |
| A | GLY220 |
| A | GLN221 |
| A | VAL224 |
| A | PRO225 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue GOL B 301 |
| Chain | Residue |
| B | ASP189 |
| B | SER190 |
| B | LYS217 |
| B | PRO219 |
| B | CYS220 |
| B | GLY220 |
| B | GLN221 |
| B | VAL224 |
| B | PRO225 |
| B | GLY226 |
| B | HOH494 |
| B | HOH531 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| A | ASP109 |
| B | VAL47 |
| B | HIS48 |
| B | PRO49 |
| B | SER120 |
| B | SER122 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| B | HIS57 |
| B | ASN192 |
| B | GLY193 |
| B | SER195 |
| B | HOH407 |
| B | HOH529 |
| B | HOH613 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue GOL C 301 |
| Chain | Residue |
| C | ASP189 |
| C | SER190 |
| C | LYS217 |
| C | CYS220 |
| C | GLY220 |
| C | GLN221 |
| C | VAL224 |
| C | PRO225 |
| C | GLY226 |
| C | HOH447 |
| C | HOH479 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue GOL D 301 |
| Chain | Residue |
| D | ASP189 |
| D | SER190 |
| D | LYS217 |
| D | CYS220 |
| D | GLY220 |
| D | GLN221 |
| D | VAL224 |
| D | PRO225 |
| D | GLY226 |
| D | HOH440 |
| D | HOH444 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL D 302 |
| Chain | Residue |
| C | ASP109 |
| D | VAL47 |
| D | HIS48 |
| D | PRO49 |
| D | SER120 |
| D | SER122 |
| D | HOH560 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 303 |
| Chain | Residue |
| D | HIS57 |
| D | ASN192 |
| D | GLY193 |
| D | SER195 |
| D | HOH422 |
| D | HOH471 |
| D | HOH519 |
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:0000269|PubMed:16950394 |
| 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 | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16950394 |
| Chain | Residue | Details |
| A | HIS25 | |
| A | GLU77 | |
| B | HIS25 | |
| B | GLU77 | |
| C | HIS25 | |
| C | GLU77 | |
| D | HIS25 | |
| D | GLU77 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN159 | |
| B | ASN159 | |
| C | ASN159 | |
| D | ASN159 |
