6X7L

LnmK in complex with 2-nitronate-propionyl-CoA

Summary for 6X7L

Entry DOI	10.2210/pdb6x7l/pdb
Descriptor	Bifunctional methylmalonyl-CoA:ACP acyltransferase/decarboxylase, ALANINE, [1-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethylsulfanyl]-1-oxidanylidene-propan-2-ylidene]-bis(oxidanidyl)azanium, ... (5 entities in total)
Functional Keywords	transferase, lyase, inhibitor, isostere, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological source	Streptomyces atroolivaceus
Total number of polymer chains	1
Total formula weight	36913.44
Authors	Stunkard, L.M.,Kick, B.J.,Lohman, J.R. (deposition date: 2020-05-30, release date: 2020-06-10, Last modification date: 2023-10-18)
Primary citation	Stunkard, L.M.,Kick, B.J.,Lohman, J.R. Structures of LnmK, a Bifunctional Acyltransferase/Decarboxylase, with Substrate Analogues Reveal the Basis for Selectivity and Stereospecificity. Biochemistry, 60:365-372, 2021 Cited by PubMed: 33482062 DOI: 10.1021/acs.biochem.0c00893 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.77 Å)

Structure validation