4KM4
E. coli alkaline phosphatase mutant S102G/R166S in complex with inorganic phosphate
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 | 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 | 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 | 12 | 
| Details | BINDING SITE FOR RESIDUE PO4 A 501 | 
| Chain | Residue | 
| A | ASP51 | 
| A | ZN502 | 
| A | ZN503 | 
| A | ZN504 | 
| A | GLY102 | 
| A | ASP153 | 
| A | ASP327 | 
| A | LYS328 | 
| A | HIS331 | 
| A | ASP369 | 
| A | HIS370 | 
| A | HIS412 | 
| site_id | AC2 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN A 502 | 
| Chain | Residue | 
| A | ASP51 | 
| A | ASP327 | 
| A | ASP369 | 
| A | HIS370 | 
| A | PO4501 | 
| site_id | AC3 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN A 503 | 
| Chain | Residue | 
| A | ASP327 | 
| A | HIS331 | 
| A | HIS412 | 
| A | PO4501 | 
| site_id | AC4 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN A 504 | 
| Chain | Residue | 
| A | ASP51 | 
| A | ASP153 | 
| A | THR155 | 
| A | GLU322 | 
| A | PO4501 | 
| site_id | AC5 | 
| Number of Residues | 11 | 
| Details | BINDING SITE FOR RESIDUE PO4 B 501 | 
| Chain | Residue | 
| B | ASP51 | 
| B | GLY102 | 
| B | ASP153 | 
| B | ASP327 | 
| B | LYS328 | 
| B | HIS331 | 
| B | ASP369 | 
| B | HIS370 | 
| B | HIS412 | 
| B | ZN502 | 
| B | ZN503 | 
| site_id | AC6 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE ZN B 502 | 
| Chain | Residue | 
| B | ASP51 | 
| B | ASP327 | 
| B | ASP369 | 
| B | HIS370 | 
| B | PO4501 | 
| site_id | AC7 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN B 503 | 
| Chain | Residue | 
| B | ASP327 | 
| B | HIS331 | 
| B | HIS412 | 
| B | PO4501 | 
| site_id | AC8 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE ZN B 504 | 
| Chain | Residue | 
| B | ASP51 | 
| B | ASP153 | 
| B | THR155 | 
| B | GLU322 | 
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 | GLY102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor | 
| A | ASP153 | metal ligand | 
| A | THR155 | metal ligand | 
| A | SER166 | 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 | GLY102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor | 
| B | ASP153 | metal ligand | 
| B | THR155 | metal ligand | 
| B | SER166 | activator, electrostatic stabiliser, hydrogen bond donor | 
| B | GLU322 | metal ligand | 
| B | ASP327 | metal ligand | 
| B | LYS328 | metal ligand | 
| B | HIS331 | metal ligand | 






