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6IJB

Structure of 3-methylmercaptopropionate CoA ligase mutant K523A in complex with AMP and MMPA

Summary for 6IJB
Entry DOI10.2210/pdb6ijb/pdb
DescriptorAMP-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 Keywordscoa ligase, atp dependent, comformational change, ligase
Biological sourceRuegeria lacuscaerulensis (strain DSM 11314 / KCTC 2953 / ITI-1157) (Silicibacter lacuscaerulensis)
Total number of polymer chains2
Total formula weight119564.47
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 citationShao, 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: 30677184
DOI: 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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