2QTC
E. coli Pyruvate dehydrogenase E1 component E401K mutant with phosphonolactylthiamin diphosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0003824 | molecular_function | catalytic activity |
A | 0004738 | molecular_function | pyruvate dehydrogenase activity |
A | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005829 | cellular_component | cytosol |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0036094 | molecular_function | small molecule binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0042867 | biological_process | pyruvate catabolic process |
A | 0045254 | cellular_component | pyruvate dehydrogenase complex |
A | 0046872 | molecular_function | metal ion binding |
A | 0060090 | molecular_function | molecular adaptor activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0004738 | molecular_function | pyruvate dehydrogenase activity |
B | 0004739 | molecular_function | pyruvate dehydrogenase (acetyl-transferring) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005829 | cellular_component | cytosol |
B | 0016020 | cellular_component | membrane |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0036094 | molecular_function | small molecule binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0042867 | biological_process | pyruvate catabolic process |
B | 0045254 | cellular_component | pyruvate dehydrogenase complex |
B | 0046872 | molecular_function | metal ion binding |
B | 0060090 | molecular_function | molecular adaptor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 888 |
Chain | Residue |
B | ASP230 |
B | ASN260 |
B | GLN262 |
B | TDK887 |
B | HOH954 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 888 |
Chain | Residue |
A | HOH896 |
A | ASP230 |
A | ASN260 |
A | GLN262 |
A | TDK887 |
site_id | AC3 |
Number of Residues | 31 |
Details | BINDING SITE FOR RESIDUE TDK B 887 |
Chain | Residue |
A | ASP521 |
A | GLU522 |
A | ILE569 |
A | GLU571 |
A | TYR599 |
A | PHE602 |
A | ARG606 |
A | GLU636 |
A | HIS640 |
B | HIS106 |
B | SER109 |
B | GLN140 |
B | HIS142 |
B | TYR177 |
B | VAL192 |
B | SER193 |
B | MET194 |
B | GLY229 |
B | ASP230 |
B | GLY231 |
B | GLU232 |
B | GLU235 |
B | ASN260 |
B | GLN262 |
B | ARG263 |
B | LEU264 |
B | LYS392 |
B | MG888 |
B | HOH925 |
B | HOH954 |
B | HOH1061 |
site_id | AC4 |
Number of Residues | 28 |
Details | BINDING SITE FOR RESIDUE TDK A 887 |
Chain | Residue |
A | HIS106 |
A | SER109 |
A | GLN140 |
A | HIS142 |
A | TYR177 |
A | VAL192 |
A | MET194 |
A | GLY229 |
A | ASP230 |
A | GLY231 |
A | GLU232 |
A | GLU235 |
A | ASN260 |
A | GLN262 |
A | ARG263 |
A | LYS392 |
A | MG888 |
A | HOH896 |
B | ASP521 |
B | GLU522 |
B | ILE569 |
B | GLU571 |
B | TYR599 |
B | PHE602 |
B | ARG606 |
B | GLU636 |
B | HIS640 |
B | HOH1035 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP230 | |
A | ASN260 | |
A | GLN262 | |
B | ASP230 | |
B | ASN260 | |
B | GLN262 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | LYS715 | |
B | LYS715 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ni4 |
Chain | Residue | Details |
A | HIS646 | |
A | GLU571 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ni4 |
Chain | Residue | Details |
B | HIS646 | |
B | GLU571 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ni4 |
Chain | Residue | Details |
A | HIS106 | |
A | HIS336 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ni4 |
Chain | Residue | Details |
B | HIS106 | |
B | HIS336 |