Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006564 | biological_process | L-serine biosynthetic process |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0016311 | biological_process | dephosphorylation |
A | 0016787 | molecular_function | hydrolase activity |
A | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006564 | biological_process | L-serine biosynthetic process |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0016311 | biological_process | dephosphorylation |
B | 0016787 | molecular_function | hydrolase activity |
B | 0036424 | molecular_function | L-phosphoserine phosphatase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PO4 A 220 |
Chain | Residue |
A | ASP11 |
A | HOH222 |
A | HOH830 |
A | PHE12 |
A | ASP13 |
A | SER99 |
A | GLY100 |
A | GLY101 |
A | LYS144 |
A | ASN170 |
A | MG221 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 221 |
Chain | Residue |
A | ASP11 |
A | ASP13 |
A | ASP167 |
A | PO4220 |
A | HOH222 |
A | HOH223 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 B 720 |
Chain | Residue |
B | ASP511 |
B | PHE512 |
B | ASP513 |
B | SER599 |
B | GLY600 |
B | LYS644 |
B | ASN670 |
B | MG721 |
B | HOH722 |
B | HOH943 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 721 |
Chain | Residue |
B | ASP511 |
B | ASP513 |
B | ASP667 |
B | PO4720 |
B | HOH722 |
B | HOH723 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PO4 B 230 |
Chain | Residue |
A | LYS4 |
B | ASN548 |
B | GLU550 |
B | HOH952 |
B | HOH962 |
B | HOH1065 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PO4 B 240 |
Chain | Residue |
B | ASN607 |
B | LYS610 |
B | GLU611 |
B | LYS691 |
B | CYS697 |
B | GLU699 |
B | HOH1064 |
B | HOH1088 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP11 | |
B | ASP511 | |
Chain | Residue | Details |
A | ASP13 | |
B | ASP513 | |
Chain | Residue | Details |
A | ASP11 | |
B | GLU520 | |
B | ARG556 | |
B | SER599 | |
B | LYS644 | |
B | ASP667 | |
A | ASP13 | |
A | GLU20 | |
A | ARG56 | |
A | SER99 | |
A | LYS144 | |
A | ASP167 | |
B | ASP511 | |
B | ASP513 | |
Chain | Residue | Details |
A | ASN170 | |
B | ASN670 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 727 |
Chain | Residue | Details |
A | ASP11 | covalently attached, metal ligand, nucleofuge, nucleophile |
A | PHE12 | electrostatic stabiliser |
A | ASP13 | metal ligand, proton acceptor, proton donor |
A | GLY100 | electrostatic stabiliser |
A | LYS144 | electrostatic stabiliser |
A | ASP171 | electrostatic stabiliser, metal ligand |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 727 |
Chain | Residue | Details |
B | ASP511 | covalently attached, metal ligand, nucleofuge, nucleophile |
B | PHE512 | electrostatic stabiliser |
B | ASP513 | metal ligand, proton acceptor, proton donor |
B | GLY600 | electrostatic stabiliser |
B | LYS644 | electrostatic stabiliser |
B | ASP671 | electrostatic stabiliser, metal ligand |