7WGR
Cryo-electron microscopic structure of the 2-oxoglutarate dehydrogenase (E1) component of the human alpha-ketoglutarate (2-oxoglutarate) dehydrogenase 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 | 12 |
Details | BINDING: BINDING => ECO:0000305|PubMed:24495017 |
Chain | Residue | Details |
A | ASP154 | |
B | GLU179 | |
B | ASP181 | |
B | ASP183 | |
A | ASP156 | |
A | ASP158 | |
A | GLU179 | |
A | ASP181 | |
A | ASP183 | |
B | ASP154 | |
B | ASP156 | |
B | ASP158 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q60597 |
Chain | Residue | Details |
A | LYS401 | |
B | LYS401 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q60597 |
Chain | Residue | Details |
A | LYS564 | |
B | LYS564 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS970 | |
B | LYS970 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:17370265 |
Chain | Residue | Details |
A | LYS534 | |
B | LYS534 |