Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003993 | molecular_function | acid phosphatase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0008199 | molecular_function | ferric iron binding |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0003993 | molecular_function | acid phosphatase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0008199 | molecular_function | ferric iron binding |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0003993 | molecular_function | acid phosphatase activity |
C | 0005576 | cellular_component | extracellular region |
C | 0008199 | molecular_function | ferric iron binding |
C | 0008270 | molecular_function | zinc ion binding |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0003993 | molecular_function | acid phosphatase activity |
D | 0005576 | cellular_component | extracellular region |
D | 0008199 | molecular_function | ferric iron binding |
D | 0008270 | molecular_function | zinc ion binding |
D | 0016787 | molecular_function | hydrolase activity |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | ATA |
Number of Residues | 2 |
Details | |
site_id | ATB |
Number of Residues | 2 |
Details | |
site_id | ATC |
Number of Residues | 2 |
Details | |
site_id | ATD |
Number of Residues | 2 |
Details | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | HIS323 | |
B | HIS323 | |
C | HIS323 | |
D | HIS323 | |
Chain | Residue | Details |
A | VAL162 | |
B | PRO194 | |
B | GLU228 | |
B | LYS313 | |
B | ASP350 | |
B | SER352 | |
C | VAL162 | |
C | ALA191 | |
C | PRO194 | |
C | GLU228 | |
C | LYS313 | |
A | ALA191 | |
C | ASP350 | |
C | SER352 | |
D | VAL162 | |
D | ALA191 | |
D | PRO194 | |
D | GLU228 | |
D | LYS313 | |
D | ASP350 | |
D | SER352 | |
A | PRO194 | |
A | GLU228 | |
A | LYS313 | |
A | ASP350 | |
A | SER352 | |
B | VAL162 | |
B | ALA191 | |
Chain | Residue | Details |
A | GLY23 | |
B | GLY23 | |
C | GLY23 | |
D | GLY23 | |
Chain | Residue | Details |
A | ARG108 | |
B | ARG108 | |
C | ARG108 | |
D | ARG108 | |
Chain | Residue | Details |
A | LEU136 | |
D | LEU136 | |
D | ARG170 | |
D | ARG423 | |
A | ARG170 | |
A | ARG423 | |
B | LEU136 | |
B | ARG170 | |
B | ARG423 | |
C | LEU136 | |
C | ARG170 | |
C | ARG423 | |
Chain | Residue | Details |
A | TYR238 | |
B | TYR238 | |
C | TYR238 | |
D | TYR238 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 4kbp |
Chain | Residue | Details |
A | HIS296 | |
A | HIS202 | |
A | HIS295 | |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 4kbp |
Chain | Residue | Details |
B | HIS296 | |
B | HIS202 | |
B | HIS295 | |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 4kbp |
Chain | Residue | Details |
C | HIS296 | |
C | HIS202 | |
C | HIS295 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 4kbp |
Chain | Residue | Details |
D | HIS296 | |
D | HIS202 | |
D | HIS295 | |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 43 |
Chain | Residue | Details |
A | VAL162 | metal ligand |
A | SER352 | metal ligand |
A | ALA191 | metal ligand |
A | PRO194 | metal ligand |
A | GLU228 | metal ligand |
A | ALA229 | electrostatic stabiliser, hydrogen bond donor |
A | LYS313 | metal ligand |
A | GLY322 | electrostatic stabiliser, hydrogen bond donor |
A | HIS323 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
A | ASP350 | metal ligand |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 43 |
Chain | Residue | Details |
B | VAL162 | metal ligand |
B | SER352 | metal ligand |
B | ALA191 | metal ligand |
B | PRO194 | metal ligand |
B | GLU228 | metal ligand |
B | ALA229 | electrostatic stabiliser, hydrogen bond donor |
B | LYS313 | metal ligand |
B | GLY322 | electrostatic stabiliser, hydrogen bond donor |
B | HIS323 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
B | ASP350 | metal ligand |
site_id | MCSA3 |
Number of Residues | 10 |
Details | M-CSA 43 |
Chain | Residue | Details |
C | VAL162 | metal ligand |
C | SER352 | metal ligand |
C | ALA191 | metal ligand |
C | PRO194 | metal ligand |
C | GLU228 | metal ligand |
C | ALA229 | electrostatic stabiliser, hydrogen bond donor |
C | LYS313 | metal ligand |
C | GLY322 | electrostatic stabiliser, hydrogen bond donor |
C | HIS323 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
C | ASP350 | metal ligand |
site_id | MCSA4 |
Number of Residues | 10 |
Details | M-CSA 43 |
Chain | Residue | Details |
D | VAL162 | metal ligand |
D | SER352 | metal ligand |
D | ALA191 | metal ligand |
D | PRO194 | metal ligand |
D | GLU228 | metal ligand |
D | ALA229 | electrostatic stabiliser, hydrogen bond donor |
D | LYS313 | metal ligand |
D | GLY322 | electrostatic stabiliser, hydrogen bond donor |
D | HIS323 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton donor |
D | ASP350 | metal ligand |