4YR1
Crystal Structure of E. Coli Alkaline Phosphatase D101A/D153A 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 | 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 | 6 |
Details | binding site for residue ZN A 501 |
Chain | Residue |
A | ASP51 |
A | SER102 |
A | ASP327 |
A | ASP369 |
A | HIS370 |
A | PO4503 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 502 |
Chain | Residue |
A | PO4503 |
A | ASP327 |
A | HIS331 |
A | HIS412 |
site_id | AC3 |
Number of Residues | 11 |
Details | binding site for residue PO4 A 503 |
Chain | Residue |
A | ASP51 |
A | SER102 |
A | ASP327 |
A | LYS328 |
A | HIS331 |
A | ASP369 |
A | HIS370 |
A | HIS412 |
A | ZN501 |
A | ZN502 |
A | HOH655 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | TYR440 |
A | GOL506 |
B | ARG23 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | ALA101 |
A | ALA103 |
A | ASN117 |
A | GLY118 |
A | ARG166 |
A | HOH605 |
A | HOH615 |
A | HOH655 |
A | HOH694 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | LYS443 |
A | SER450 |
A | GOL504 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN B 501 |
Chain | Residue |
B | ASP327 |
B | HIS331 |
B | HIS412 |
B | PO4503 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue ZN B 502 |
Chain | Residue |
B | ASP51 |
B | ASP327 |
B | ASP369 |
B | HIS370 |
B | PO4503 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue PO4 B 503 |
Chain | Residue |
B | ASP51 |
B | ALA101 |
B | SER102 |
B | ARG166 |
B | ASP327 |
B | LYS328 |
B | HIS331 |
B | ASP369 |
B | HIS370 |
B | HIS412 |
B | ZN501 |
B | ZN502 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
B | ALA101 |
B | ASN117 |
B | GLY118 |
B | ARG166 |
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 | ALA153 | |
B | THR155 | |
B | GLU322 | |
B | ASP327 | |
B | HIS331 | |
B | ASP369 | |
B | HIS370 | |
B | HIS412 | |
A | ALA153 | |
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 | ALA153 | 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 | ALA153 | 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 |