6VEF
Cryo-EM Structure of Escherichia coli 2-oxoglutarate dehydrogenase E1 component sucA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 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 | 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 | 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 | 9 |
| Details | binding site for residue AMP A 1001 |
| Chain | Residue |
| A | HIS313 |
| A | ARG337 |
| A | SER530 |
| A | PHE531 |
| A | TRP533 |
| A | LEU537 |
| A | THR673 |
| A | ARG710 |
| A | MET711 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue OAA A 1002 |
| Chain | Residue |
| A | GLU616 |
| A | LEU659 |
| A | GLN685 |
| A | PHE689 |
| B | HIS260 |
| B | ARG261 |
| B | ASP357 |
| B | GLY393 |
| B | PHE394 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue OAA B 1001 |
| Chain | Residue |
| A | HIS260 |
| A | ARG261 |
| A | ASP357 |
| A | GLY393 |
| A | PHE394 |
| B | GLU616 |
| B | LEU659 |
| B | GLN685 |
| B | PHE689 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue AMP B 1002 |
| Chain | Residue |
| B | HIS313 |
| B | ARG337 |
| B | SER530 |
| B | PHE531 |
| B | TRP533 |
| B | LEU537 |
| B | THR673 |
| B | ARG710 |
| B | MET711 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"O-AMP-threonine; by ydiU","evidences":[{"source":"PubMed","id":"30270044","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
