Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0002020 | molecular_function | protease binding |
A | 0004035 | molecular_function | alkaline phosphatase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005886 | cellular_component | plasma membrane |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009897 | cellular_component | external side of plasma membrane |
A | 0016311 | biological_process | dephosphorylation |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016791 | molecular_function | phosphatase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0071773 | biological_process | cellular response to BMP stimulus |
A | 0098552 | cellular_component | side of membrane |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0002020 | molecular_function | protease binding |
B | 0004035 | molecular_function | alkaline phosphatase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005886 | cellular_component | plasma membrane |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009897 | cellular_component | external side of plasma membrane |
B | 0016311 | biological_process | dephosphorylation |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016791 | molecular_function | phosphatase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0071773 | biological_process | cellular response to BMP stimulus |
B | 0098552 | cellular_component | side of membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 501 |
Chain | Residue |
A | SER155 |
A | GLU311 |
A | HOH734 |
A | HOH735 |
A | HOH736 |
A | HOH737 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | ASP285 |
A | HOH634 |
A | GLU216 |
A | PHE269 |
A | GLU270 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 503 |
Chain | Residue |
A | LYS34 |
A | ASN35 |
A | SER300 |
A | THR345 |
A | ASN346 |
A | ASP349 |
A | THR350 |
A | HOH651 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 501 |
Chain | Residue |
B | SER155 |
B | GLU311 |
B | HOH704 |
B | HOH737 |
B | HOH738 |
B | HOH739 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 502 |
Chain | Residue |
B | GLU216 |
B | PHE269 |
B | GLU270 |
B | ASP285 |
B | HOH609 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 503 |
Chain | Residue |
B | LYS34 |
B | ASN35 |
B | SER300 |
B | ASN346 |
B | ASP349 |
B | THR350 |
B | HOH631 |
Functional Information from PROSITE/UniProt
site_id | PS00123 |
Number of Residues | 9 |
Details | ALKALINE_PHOSPHATASE Alkaline phosphatase active site. VpDSAGTAT |
Chain | Residue | Details |
A | VAL89-THR97 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SEP92 | |
B | SEP92 | |
Chain | Residue | Details |
A | ASP42 | |
B | ASP42 | |
B | SEP92 | |
B | SER155 | |
B | GLU311 | |
B | ASP316 | |
B | HIS320 | |
B | ASP357 | |
B | HIS358 | |
B | HIS432 | |
A | SEP92 | |
A | SER155 | |
A | GLU311 | |
A | ASP316 | |
A | HIS320 | |
A | ASP357 | |
A | HIS358 | |
A | HIS432 | |
Chain | Residue | Details |
A | GLU216 | |
A | PHE269 | |
A | GLU270 | |
A | ASP285 | |
B | GLU216 | |
B | PHE269 | |
B | GLU270 | |
B | ASP285 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN122 | |
B | ASN122 | |
Chain | Residue | Details |
A | ASN281 | |
A | ASN408 | |
B | ASN281 | |
B | ASN408 | |