6CT0
Atomic Structure of the E2 Inner Core of Human Pyruvate Dehydrogenase Complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 0 | 0004742 | molecular_function | dihydrolipoyllysine-residue acetyltransferase activity |
| 0 | 0005515 | molecular_function | protein binding |
| 0 | 0005739 | cellular_component | mitochondrion |
| 0 | 0005759 | cellular_component | mitochondrial matrix |
| 0 | 0006006 | biological_process | glucose metabolic process |
| 0 | 0006086 | biological_process | pyruvate decarboxylation to acetyl-CoA |
| 0 | 0006090 | biological_process | pyruvate metabolic process |
| 0 | 0006099 | biological_process | tricarboxylic acid cycle |
| 0 | 0016407 | molecular_function | acetyltransferase activity |
| 0 | 0016740 | molecular_function | transferase activity |
| 0 | 0016746 | molecular_function | acyltransferase activity |
| 0 | 0034604 | molecular_function | obsolete pyruvate dehydrogenase (NAD+) activity |
| 0 | 0042802 | molecular_function | identical protein binding |
| 0 | 0042867 | biological_process | pyruvate catabolic process |
| 0 | 0045254 | cellular_component | pyruvate dehydrogenase complex |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 12 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PalSPtMTMGTV |
| Chain | Residue | Details |
| 0 | PRO224-VAL235 |
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GdkInegDLIaeVETdKATvgFesleeCyM |
| Chain | Residue | Details |
| 0 | GLY116-MET145 | |
| 0 | GLY243-LEU272 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q9N0F1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11181","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BMF4","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






