8I0K
Cryo-electron microscopic structure of the 2-oxoglutarate dehydrogenase(E1) with TCAIM complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
| 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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"35272141","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7WGR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q60597","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q60597","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"17370265","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 33 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
