6IJB
Structure of 3-methylmercaptopropionate CoA ligase mutant K523A in complex with AMP and MMPA
Summary for 6IJB
Entry DOI | 10.2210/pdb6ijb/pdb |
Descriptor | AMP-binding domain protein, ADENOSINE MONOPHOSPHATE, 2-[3-(2-HYDROXY-1,1-DIHYDROXYMETHYL-ETHYLAMINO)-PROPYLAMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total) |
Functional Keywords | coa ligase, atp dependent, comformational change, ligase |
Biological source | Ruegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis) |
Total number of polymer chains | 2 |
Total formula weight | 119564.47 |
Authors | Shao, X.,Cao, H.Y.,Wang, P.,Li, C.Y.,Zhao, F.,Peng, M.,Chen, X.L.,Zhang, Y.Z. (deposition date: 2018-10-09, release date: 2019-07-03, Last modification date: 2023-11-22) |
Primary citation | Shao, X.,Cao, H.Y.,Zhao, F.,Peng, M.,Wang, P.,Li, C.Y.,Shi, W.L.,Wei, T.D.,Yuan, Z.,Zhang, X.H.,Chen, X.L.,Todd, J.D.,Zhang, Y.Z. Mechanistic insight into 3-methylmercaptopropionate metabolism and kinetical regulation of demethylation pathway in marine dimethylsulfoniopropionate-catabolizing bacteria. Mol.Microbiol., 111:1057-1073, 2019 Cited by PubMed: 30677184DOI: 10.1111/mmi.14211 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.111 Å) |
Structure validation
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