2JGD
E. COLI 2-oxoglutarate dehydrogenase (E1o)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004591 | molecular_function | oxoglutarate dehydrogenase (succinyl-transferring) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006099 | biological_process | tricarboxylic acid cycle |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
A | 0030976 | molecular_function | thiamine pyrophosphate binding |
A | 0042802 | molecular_function | identical protein binding |
A | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
B | 0000166 | molecular_function | nucleotide binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004591 | molecular_function | oxoglutarate dehydrogenase (succinyl-transferring) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006099 | biological_process | tricarboxylic acid cycle |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016624 | molecular_function | oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor |
B | 0030976 | molecular_function | thiamine pyrophosphate binding |
B | 0042802 | molecular_function | identical protein binding |
B | 0045252 | cellular_component | oxoglutarate dehydrogenase complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE AMP A1934 |
Chain | Residue |
A | SER302 |
A | GLY709 |
A | ARG710 |
A | MET711 |
A | HOH2145 |
A | HOH2146 |
A | HOH2335 |
A | HOH2336 |
A | HOH2337 |
A | HIS313 |
A | ALA315 |
A | ARG337 |
A | MET526 |
A | SER530 |
A | PHE531 |
A | TRP533 |
A | THR673 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE AMP B1934 |
Chain | Residue |
B | SER302 |
B | HIS313 |
B | ALA315 |
B | ARG337 |
B | SER530 |
B | PHE531 |
B | TRP533 |
B | THR673 |
B | GLY709 |
B | ARG710 |
B | MET711 |
B | HOH2394 |
B | HOH2395 |
B | HOH2396 |
B | HOH2397 |
B | HOH2398 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: O-AMP-threonine; by ydiU => ECO:0000269|PubMed:30270044 |
Chain | Residue | Details |
B | THR405 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dtw |
Chain | Residue | Details |
A | GLU661 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1dtw |
Chain | Residue | Details |
B | GLU661 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dtw |
Chain | Residue | Details |
A | SER730 | |
A | GLU661 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1dtw |
Chain | Residue | Details |
B | SER730 | |
B | GLU661 |