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E. COLI ALKALINE PHOSPHATASE MUTANT (S102C)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004035 | molecular_function | alkaline phosphatase activity |
A | 0004721 | molecular_function | phosphoprotein phosphatase activity |
A | 0005515 | molecular_function | protein binding |
A | 0006470 | biological_process | protein dephosphorylation |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016791 | molecular_function | phosphatase activity |
A | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
A | 0030613 | molecular_function | oxidoreductase activity, acting on phosphorus or arsenic in donors |
A | 0033748 | molecular_function | hydrogenase (acceptor) activity |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004035 | molecular_function | alkaline phosphatase activity |
B | 0004721 | molecular_function | phosphoprotein phosphatase activity |
B | 0005515 | molecular_function | protein binding |
B | 0006470 | biological_process | protein dephosphorylation |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016791 | molecular_function | phosphatase activity |
B | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
B | 0030613 | molecular_function | oxidoreductase activity, acting on phosphorus or arsenic in donors |
B | 0033748 | molecular_function | hydrogenase (acceptor) activity |
B | 0042597 | cellular_component | periplasmic space |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 450 |
Chain | Residue |
A | ASP327 |
A | HIS331 |
A | HIS372 |
A | HIS412 |
A | PO4453 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 451 |
Chain | Residue |
A | ASP51 |
A | CYS102 |
A | ASP369 |
A | HIS370 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 452 |
Chain | Residue |
A | ASP51 |
A | THR155 |
A | GLU322 |
A | HOH454 |
A | HOH455 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 453 |
Chain | Residue |
A | CYS102 |
A | ASP327 |
A | HIS331 |
A | HIS412 |
A | ZN450 |
A | HOH633 |
A | HOH634 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN B 450 |
Chain | Residue |
B | CYS102 |
B | ASP327 |
B | HIS331 |
B | HIS412 |
B | PO4453 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 451 |
Chain | Residue |
B | ASP51 |
B | CYS102 |
B | ASP369 |
B | HIS370 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG B 452 |
Chain | Residue |
B | ASP51 |
B | ASP153 |
B | THR155 |
B | GLU322 |
B | HOH454 |
B | HOH455 |
B | HOH456 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 B 453 |
Chain | Residue |
B | ASP101 |
B | CYS102 |
B | ARG166 |
B | ASP327 |
B | HIS331 |
B | HIS412 |
B | ZN450 |
B | HOH466 |
B | HOH653 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Phosphoserine intermediate |
Chain | Residue | Details |
A | CYS102 | |
B | CYS102 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP51 | |
B | ASP51 | |
B | ASP153 | |
B | THR155 | |
B | GLU322 | |
B | ASP327 | |
B | HIS331 | |
B | ASP369 | |
B | HIS370 | |
B | HIS412 | |
A | ASP153 | |
A | THR155 | |
A | GLU322 | |
A | ASP327 | |
A | HIS331 | |
A | ASP369 | |
A | HIS370 | |
A | HIS412 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1alk |
Chain | Residue | Details |
A | CYS102 | |
A | ARG166 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1alk |
Chain | Residue | Details |
B | CYS102 | |
B | ARG166 |
site_id | MCSA1 |
Number of Residues | 12 |
Details | M-CSA 44 |
Chain | Residue | Details |
A | ASP51 | metal ligand |
A | ASP369 | metal ligand |
A | HIS370 | metal ligand |
A | HIS412 | metal ligand |
A | CYS102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
A | ASP153 | metal ligand |
A | THR155 | metal ligand |
A | ARG166 | activator, electrostatic stabiliser, hydrogen bond donor |
A | GLU322 | metal ligand |
A | ASP327 | metal ligand |
A | LYS328 | metal ligand |
A | HIS331 | metal ligand |
site_id | MCSA2 |
Number of Residues | 12 |
Details | M-CSA 44 |
Chain | Residue | Details |
B | ASP51 | metal ligand |
B | ASP369 | metal ligand |
B | HIS370 | metal ligand |
B | HIS412 | metal ligand |
B | CYS102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
B | ASP153 | metal ligand |
B | THR155 | metal ligand |
B | ARG166 | activator, electrostatic stabiliser, hydrogen bond donor |
B | GLU322 | metal ligand |
B | ASP327 | metal ligand |
B | LYS328 | metal ligand |
B | HIS331 | metal ligand |