1ED8
STRUCTURE OF E. COLI ALKALINE PHOSPHATASE INHIBITED BY THE INORGANIC PHOSPHATE AT 1.75A RESOLUTION
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 | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 450 |
Chain | Residue |
A | ASP327 |
A | HIS331 |
A | HIS412 |
A | PO4456 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 451 |
Chain | Residue |
A | PO4456 |
A | ASP51 |
A | SER102 |
A | ASP327 |
A | ASP369 |
A | HIS370 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN A 452 |
Chain | Residue |
A | ASP51 |
A | THR155 |
A | GLU322 |
A | HOH453 |
A | HOH454 |
A | HOH455 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 462 |
Chain | Residue |
A | ASP51 |
A | THR155 |
A | GLU322 |
A | HOH453 |
A | HOH454 |
A | HOH455 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PO4 A 456 |
Chain | Residue |
A | ASP51 |
A | SER102 |
A | ARG166 |
A | ASP327 |
A | HIS331 |
A | ASP369 |
A | HIS370 |
A | HIS412 |
A | ZN450 |
A | ZN451 |
A | HOH453 |
A | HOH1045 |
A | HOH1093 |
A | HOH1603 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 458 |
Chain | Residue |
A | ARG267 |
A | TRP268 |
A | ARG292 |
A | HOH1465 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 950 |
Chain | Residue |
B | ASP827 |
B | HIS831 |
B | HIS912 |
B | PO4956 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 951 |
Chain | Residue |
B | ASP551 |
B | SER602 |
B | ASP827 |
B | ASP869 |
B | HIS870 |
B | PO4956 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN B 952 |
Chain | Residue |
B | ASP551 |
B | THR655 |
B | GLU822 |
B | HOH953 |
B | HOH954 |
B | HOH955 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 962 |
Chain | Residue |
B | ASP551 |
B | THR655 |
B | GLU822 |
B | HOH953 |
B | HOH954 |
B | HOH955 |
site_id | BC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PO4 B 956 |
Chain | Residue |
B | ASP551 |
B | ASP601 |
B | SER602 |
B | ARG666 |
B | ASP827 |
B | HIS831 |
B | ASP869 |
B | HIS870 |
B | HIS912 |
B | ZN950 |
B | ZN951 |
B | HOH953 |
B | HOH1095 |
B | HOH1602 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 958 |
Chain | Residue |
B | ARG767 |
B | TRP768 |
B | ARG792 |
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 | SER602 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP51 | |
B | ASP551 | |
B | ASP653 | |
B | THR655 | |
B | GLU822 | |
B | ASP827 | |
B | HIS831 | |
B | ASP869 | |
B | HIS870 | |
B | HIS912 | |
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 | SER102 | |
A | ARG166 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1alk |
Chain | Residue | Details |
B | SER602 | |
B | ARG666 |
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 | ASP551 | metal ligand |
B | ASP869 | metal ligand |
B | HIS870 | metal ligand |
B | HIS912 | metal ligand |
B | SER602 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
B | ASP653 | metal ligand |
B | THR655 | metal ligand |
B | ARG666 | activator, electrostatic stabiliser, hydrogen bond donor |
B | GLU822 | metal ligand |
B | ASP827 | metal ligand |
B | LYS828 | metal ligand |
B | HIS831 | metal ligand |