2IOF
Crystal structure of phosphonoacetaldehyde hydrolase with sodium borohydride-reduced substrate intermediate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0019700 | biological_process | organic phosphonate catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0050194 | molecular_function | phosphonoacetaldehyde hydrolase activity |
K | 0000287 | molecular_function | magnesium ion binding |
K | 0003824 | molecular_function | catalytic activity |
K | 0016787 | molecular_function | hydrolase activity |
K | 0019700 | biological_process | organic phosphonate catabolic process |
K | 0046872 | molecular_function | metal ion binding |
K | 0050194 | molecular_function | phosphonoacetaldehyde hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 361 |
Chain | Residue |
A | ASP12 |
A | ALA14 |
A | GLY50 |
A | LYS53 |
A | THR126 |
A | GLY127 |
A | MG462 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 462 |
Chain | Residue |
A | ASP186 |
A | PO4361 |
A | ASP12 |
A | ALA14 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PO4 K 361 |
Chain | Residue |
K | ASP12 |
K | TRP13 |
K | ALA14 |
K | THR126 |
K | GLY127 |
K | ARG160 |
K | MG462 |
K | HOH535 |
K | HOH536 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG K 462 |
Chain | Residue |
K | ASP12 |
K | ALA14 |
K | ASP186 |
K | PO4361 |
K | HOH535 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
K | ASP12 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Schiff-base intermediate with substrate |
Chain | Residue | Details |
K | LDH53 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
K | ASP12 | |
K | ALA14 | |
K | ASP186 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
A | THR126 | |
A | ARG160 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
K | THR126 | |
K | ARG160 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
A | MET49 | |
A | HIS56 | |
A | LYS53 | |
A | ALA45 | |
A | ASP12 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1lvh |
Chain | Residue | Details |
K | MET49 | |
K | HIS56 | |
K | ALA45 | |
K | ASP12 |
site_id | MCSA1 |
Number of Residues | 8 |
Details | M-CSA 181 |
Chain | Residue | Details |
K | ASP12 | hydrogen bond acceptor, metal ligand, nucleofuge, nucleophile |
K | ALA14 | metal ligand |
K | ALA45 | electrostatic stabiliser, hydrogen bond acceptor |
K | MET49 | activator, electrostatic stabiliser, hydrogen bond acceptor |
K | LDH53 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, polar interaction, proton acceptor, proton donor |
K | HIS56 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
K | ARG160 | electrostatic stabiliser, hydrogen bond donor |
K | ASP186 | metal ligand |