7PT2

Actinobacterial 2-hydroxyacyl-CoA lyase (AcHACL) mutant E493Q structure in complex with substrate 2-HIB-CoA and inactive cofactor 3-deaza-ThDP

Summary for 7PT2

• Entry DOI: 10.2210/pdb7pt2/pdb
• Descriptor: 2-hydroxyacyl-CoA lyase, 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-3-METHYLTHIOPHEN-2-YL}ETHYL TRIHYDROGEN DIPHOSPHATE, S-{(3R,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} 2-hydroxy-2-methylpropanethioate, ... (5 entities in total)
• Functional Keywords: thdp, coa, lyase
• Biological source: Actinomycetospora chiangmaiensis DSM 45062
• Total number of polymer chains: 2
• Total formula weight: 133373.44

Authors

Zahn, M.,Rohwerder, T. (deposition date: 2021-09-25, release date: 2022-02-02, Last modification date: 2022-02-09)

• Primary citation: Zahn, M.,Konig, G.,Pham, H.V.C.,Seroka, B.,Lazny, R.,Yang, G.,Ouerfelli, O.,Lotowski, Z.,Rohwerder, T.; Mechanistic details of the actinobacterial lyase-catalyzed degradation reaction of 2-hydroxyisobutyryl-CoA.; J.Biol.Chem., 298:101522-101522, 2022; PubMed: 34952003; DOI: 10.1016/j.jbc.2021.101522

Experimental method

X-RAY DIFFRACTION (1.762 Å)