4JBN

Crystal structure of O-Acetyl Serine Sulfhydrylase from Entamoeba histolytica in complex with Serine acetyl transferase derived tetrapeptide, SPSI

Summary for 4JBN

Entry DOI	10.2210/pdb4jbn/pdb
Related	2PQM 3BM5 4IL5 4JBL
Descriptor	Cysteine synthase, SAT derived tetrapeptide, SULFATE ION, ... (4 entities in total)
Functional Keywords	cysteine synthase, peptide inhibitor, plp fold type 2, tryptophan synthase family, lyase, serine acetyl transferase, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological source	Entamoeba histolytica
Total number of polymer chains	3
Total formula weight	74772.02
Authors	Raj, I.,Gourinath, S. (deposition date: 2013-02-20, release date: 2013-12-04, Last modification date: 2023-12-06)
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 (1.87 Å)

Structure validation