Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004742 | molecular_function | dihydrolipoyllysine-residue acetyltransferase activity |
| A | 0006096 | biological_process | glycolytic process |
| A | 0045254 | cellular_component | pyruvate dehydrogenase complex |
Functional Information from PDB Data
| site_id | LIP |
| Number of Residues | 1 |
| Details | LYS 39 IS THE LIPOYLATION SITE WHERE LIPOIC ACID (6,8 THIOCTIC ACID) IS COVALENTLY ATTACHED VIA AN AMIDE LINKAGE TO THE LYSINE SIDE CHAIN. |
Functional Information from PROSITE/UniProt
| site_id | PS00189 |
| Number of Residues | 30 |
| Details | LIPOYL 2-oxo acid dehydrogenases acyltransferase component lipoyl binding site. GdlIeveQGLvvLESaKASmeVpspkaGvV |
| Chain | Residue | Details |
| A | GLY23-VAL52 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Domain: {"description":"Lipoyl-binding 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-lipoyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"}]} |
