5TPQ
E. coli alkaline phosphatase D101A, D153A, R166S, E322A, K328A mutant
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 | 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 | 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 | 5 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | ASP51 |
| A | SER102 |
| A | ASP369 |
| A | HIS370 |
| A | PO4504 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | ASP327 |
| A | HIS331 |
| A | HIS412 |
| A | PO4504 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 503 |
| Chain | Residue |
| A | GLU134 |
| A | HIS162 |
| A | HIS452 |
| A | HOH720 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 504 |
| Chain | Residue |
| A | ASP51 |
| A | SER102 |
| A | ASP327 |
| A | HIS331 |
| A | HIS412 |
| A | ZN501 |
| A | ZN502 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 505 |
| Chain | Residue |
| A | ASP304 |
| A | GLU308 |
| B | HIS125 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| B | ASP51 |
| B | SER102 |
| B | ASP327 |
| B | ASP369 |
| B | HIS370 |
| B | PO4504 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 502 |
| Chain | Residue |
| B | ASP327 |
| B | HIS331 |
| B | HIS412 |
| B | PO4504 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue ZN B 503 |
| Chain | Residue |
| B | GLU134 |
| B | HIS162 |
| B | HIS452 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue PO4 B 504 |
| Chain | Residue |
| B | SER102 |
| B | ASP327 |
| B | HIS370 |
| B | HIS412 |
| B | ZN501 |
| B | ZN502 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Phosphoserine intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {} |
| Chain | Residue | Details |
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 | ALA153 | metal ligand |
| A | THR155 | metal ligand |
| A | SER166 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | ALA322 | metal ligand |
| A | ASP327 | metal ligand |
| A | ALA328 | 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 | ALA153 | metal ligand |
| B | THR155 | metal ligand |
| B | SER166 | activator, electrostatic stabiliser, hydrogen bond donor |
| B | ALA322 | metal ligand |
| B | ASP327 | metal ligand |
| B | ALA328 | metal ligand |
| B | HIS331 | metal ligand |
