4JBL

Crystal structure of O-Acetyl Serine Sulfhydrylase from Entamoeba histolytica in complex with Methionine

Summary for 4JBL

Entry DOI	10.2210/pdb4jbl/pdb
Related	2PQM 3BM5 4IL5 4JBN
Descriptor	Cysteine synthase, SULFATE ION, METHIONINE, ... (4 entities in total)
Functional Keywords	cysteine synthase, substrate analog, plp fold type 2, lyase, sulfhydrylase, serine acetyl transferase, transferase
Biological source	Entamoeba histolytica
Total number of polymer chains	2
Total formula weight	74891.14
Authors	Raj, I.,Gourinath, S. (deposition date: 2013-02-19, release date: 2013-12-04, Last modification date: 2024-03-20)
Primary citation	Raj, I.,Mazumder, M.,Gourinath, S. Molecular basis of ligand recognition by OASS from E. histolytica: insights from structural and molecular dynamics simulation studies Biochim.Biophys.Acta, 1830:4573-4583, 2013 Cited by PubMed Abstract: O-acetyl serine sulfhydrylase (OASS) is a pyridoxal phosphate (PLP) dependent enzyme catalyzing the last step of the cysteine biosynthetic pathway. Here we analyze and investigate the factors responsible for recognition and different conformational changes accompanying the binding of various ligands to OASS. PubMed: 23747298 DOI: 10.1016/j.bbagen.2013.05.041 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation