1AJD
THREE-DIMENSIONAL STRUCTURE OF THE D153G MUTANT OF E. COLI ALKALINE PHOSPHATASE: A MUTANT WITH WEAKER MAGNESIUM BINDING AND INCREASED CATALYTIC ACTIVITY
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 | 0016311 | biological_process | dephosphorylation |
| 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 | 0016311 | biological_process | dephosphorylation |
| 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 | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 450 |
| Chain | Residue |
| A | ASP327 |
| A | HIS331 |
| A | HIS412 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 451 |
| Chain | Residue |
| A | ASP369 |
| A | HIS370 |
| A | HIS412 |
| A | ASP51 |
| A | SER102 |
| A | ASP327 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 452 |
| Chain | Residue |
| A | ASP51 |
| A | THR155 |
| A | GLU322 |
| A | HOH455 |
| A | HOH456 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 950 |
| Chain | Residue |
| B | ASP327 |
| B | HIS331 |
| B | HIS412 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 951 |
| Chain | Residue |
| B | ASP51 |
| B | SER102 |
| B | ASP327 |
| B | ASP369 |
| B | HIS370 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 952 |
| Chain | Residue |
| B | ASP51 |
| B | THR155 |
| B | GLU322 |
| B | HOH955 |
| B | HOH956 |
| site_id | ACT |
| Number of Residues | 3 |
| Details | TWO ZN2+ AND ONE MG2+ IONS ARE AT THE ACTIVE-SITE. |
| Chain | Residue |
| A | ZN450 |
| A | ZN451 |
| A | MG452 |
Functional Information from PROSITE/UniProt
| site_id | PS00123 |
| Number of Residues | 9 |
| Details | ALKALINE_PHOSPHATASE Alkaline phosphatase active site. VtDSAASAT |
| Chain | Residue | Details |
| A | VAL99-THR107 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Phosphoserine intermediate |
| Chain | Residue | Details |
| A | SER102 | |
| B | SER102 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP51 | |
| B | ASP51 | |
| B | GLY153 | |
| B | THR155 | |
| B | GLU322 | |
| B | ASP327 | |
| B | HIS331 | |
| B | ASP369 | |
| B | HIS370 | |
| B | HIS412 | |
| A | GLY153 | |
| A | THR155 | |
| A | GLU322 | |
| A | ASP327 | |
| A | HIS331 | |
| A | ASP369 | |
| A | HIS370 | |
| A | HIS412 |
Catalytic Information from CSA
| 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 | SER102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY153 | 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 | SER102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | GLY153 | 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 |
