3TG0
E. coli alkaline phosphatase with bound 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 | 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 |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004035 | molecular_function | alkaline phosphatase activity |
| C | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0016311 | biological_process | dephosphorylation |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016791 | molecular_function | phosphatase activity |
| C | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| C | 0030613 | molecular_function | oxidoreductase activity, acting on phosphorus or arsenic in donors |
| C | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| C | 0042597 | cellular_component | periplasmic space |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004035 | molecular_function | alkaline phosphatase activity |
| D | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0016311 | biological_process | dephosphorylation |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016791 | molecular_function | phosphatase activity |
| D | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| D | 0030613 | molecular_function | oxidoreductase activity, acting on phosphorus or arsenic in donors |
| D | 0033748 | molecular_function | hydrogenase (acceptor) activity |
| D | 0042597 | cellular_component | periplasmic space |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | ASP51 |
| A | SER102 |
| A | ASP327 |
| A | ASP369 |
| A | HIS370 |
| A | PO4504 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | PO4504 |
| A | ASP327 |
| A | HIS331 |
| A | HIS412 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | ASP51 |
| A | THR155 |
| A | GLU322 |
| A | HOH5060 |
| A | HOH5124 |
| A | HOH5275 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PO4 A 504 |
| Chain | Residue |
| A | ASP51 |
| A | SER102 |
| A | ARG166 |
| A | ASP327 |
| A | HIS331 |
| A | HIS370 |
| A | HIS412 |
| A | ZN501 |
| A | ZN502 |
| A | HOH5189 |
| A | HOH5275 |
| A | HOH6264 |
| A | HOH6450 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 505 |
| Chain | Residue |
| B | ASP327 |
| B | HIS331 |
| B | HIS412 |
| B | PO4508 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 506 |
| Chain | Residue |
| B | ASP51 |
| B | SER102 |
| B | ASP369 |
| B | HIS370 |
| B | PO4508 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 507 |
| Chain | Residue |
| B | ASP51 |
| B | THR155 |
| B | GLU322 |
| B | HOH5001 |
| B | HOH5093 |
| B | HOH5117 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PO4 B 508 |
| Chain | Residue |
| B | ASP51 |
| B | ASP101 |
| B | SER102 |
| B | ARG166 |
| B | ASP327 |
| B | HIS331 |
| B | HIS370 |
| B | HIS412 |
| B | ZN505 |
| B | ZN506 |
| B | HOH5054 |
| B | HOH5117 |
| B | HOH6160 |
| B | HOH6503 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 509 |
| Chain | Residue |
| C | ASP51 |
| C | SER102 |
| C | ASP327 |
| C | ASP369 |
| C | HIS370 |
| C | PO4512 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 510 |
| Chain | Residue |
| C | ASP327 |
| C | HIS331 |
| C | HIS412 |
| C | PO4512 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 511 |
| Chain | Residue |
| C | ASP51 |
| C | THR155 |
| C | GLU322 |
| C | HOH5002 |
| C | HOH5232 |
| C | HOH6210 |
| site_id | BC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PO4 C 512 |
| Chain | Residue |
| C | ASP51 |
| C | SER102 |
| C | ARG166 |
| C | ASP327 |
| C | HIS331 |
| C | HIS370 |
| C | HIS412 |
| C | ZN509 |
| C | ZN510 |
| C | HOH5330 |
| C | HOH6210 |
| C | HOH6497 |
| C | HOH6614 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 513 |
| Chain | Residue |
| D | ASP51 |
| D | SER102 |
| D | ASP369 |
| D | HIS370 |
| D | PO4516 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 514 |
| Chain | Residue |
| D | ASP327 |
| D | HIS331 |
| D | HIS412 |
| D | PO4516 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 515 |
| Chain | Residue |
| D | HOH5098 |
| D | HOH5112 |
| D | HOH5158 |
| D | ASP51 |
| D | THR155 |
| D | GLU322 |
| site_id | BC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PO4 D 516 |
| Chain | Residue |
| D | ASP51 |
| D | ASP101 |
| D | SER102 |
| D | ARG166 |
| D | ASP327 |
| D | HIS331 |
| D | HIS370 |
| D | HIS412 |
| D | ZN513 |
| D | ZN514 |
| D | HOH5096 |
| D | HOH5158 |
| D | HOH6411 |
| D | HOH6715 |
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 | 4 |
| Details | Active site: {"description":"Phosphoserine intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| 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 | 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 | SER102 | 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 |
| site_id | MCSA3 |
| Number of Residues | 12 |
| Details | M-CSA 44 |
| Chain | Residue | Details |
| C | ASP51 | metal ligand |
| C | ASP369 | metal ligand |
| C | HIS370 | metal ligand |
| C | HIS412 | metal ligand |
| C | SER102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | ASP153 | metal ligand |
| C | THR155 | metal ligand |
| C | ARG166 | activator, electrostatic stabiliser, hydrogen bond donor |
| C | GLU322 | metal ligand |
| C | ASP327 | metal ligand |
| C | LYS328 | metal ligand |
| C | HIS331 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 12 |
| Details | M-CSA 44 |
| Chain | Residue | Details |
| D | ASP51 | metal ligand |
| D | ASP369 | metal ligand |
| D | HIS370 | metal ligand |
| D | HIS412 | metal ligand |
| D | SER102 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | ASP153 | metal ligand |
| D | THR155 | metal ligand |
| D | ARG166 | activator, electrostatic stabiliser, hydrogen bond donor |
| D | GLU322 | metal ligand |
| D | ASP327 | metal ligand |
| D | LYS328 | metal ligand |
| D | HIS331 | metal ligand |
