8RPL
AMP-forming acetyl-CoA synthetase from Chloroflexota bacterium with bound acetyl AMP
Summary for 8RPL
Entry DOI | 10.2210/pdb8rpl/pdb |
Descriptor | Acetate--CoA ligase, [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] ethanoate, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (6 entities in total) |
Functional Keywords | acetate, acetyl-amp, coa, phospho histidine, acsa, ligase |
Biological source | Chloroflexota bacterium |
Total number of polymer chains | 4 |
Total formula weight | 299072.22 |
Authors | Striska, K.,Palm, G.J.,Lammers, M. (deposition date: 2024-01-16, release date: 2024-06-19, Last modification date: 2024-07-31) |
Primary citation | Qin, C.,Graf, L.G.,Striska, K.,Janetzky, M.,Geist, N.,Specht, R.,Schulze, S.,Palm, G.J.,Girbardt, B.,Dorre, B.,Berndt, L.,Kemnitz, S.,Doerr, M.,Bornscheuer, U.T.,Delcea, M.,Lammers, M. Acetyl-CoA synthetase activity is enzymatically regulated by lysine acetylation using acetyl-CoA or acetyl-phosphate as donor molecule. Nat Commun, 15:6002-6002, 2024 Cited by PubMed: 39019872DOI: 10.1038/s41467-024-49952-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.37 Å) |
Structure validation
Download full validation report![Download](/newweb/media/icons/dl.png)
![Download](/newweb/media/icons/dl.png)