5ET4

Structure of RNase A-K7H/R10H in complex with 3'-CMP

Summary for 5ET4

Entry DOI	10.2210/pdb5et4/pdb
Related	4U7R
Descriptor	Ribonuclease pancreatic, CYTIDINE-3'-MONOPHOSPHATE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
Functional Keywords	rnase a, p2 subsite, exonuclease activity, hydrolase
Biological source	Bos taurus (Bovine) More
Total number of polymer chains	4
Total formula weight	56203.95
Authors	Blanco, J.A.,Salazar, V.A.,Moussaoui, M.,Boix, E. (deposition date: 2015-11-17, release date: 2016-11-30, Last modification date: 2024-11-13)
Primary citation	Prats-Ejarque, G.,Blanco, J.A.,Salazar, V.A.,Nogues, V.M.,Moussaoui, M.,Boix, E. Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates. Biochim Biophys Acta Gen Subj, 1863:105-117, 2019 Cited by PubMed Abstract: Human RNase6 is a small cationic antimicrobial protein that belongs to the vertebrate RNaseA superfamily. All members share a common catalytic mechanism, which involves a conserved catalytic triad, constituted by two histidines and a lysine (His15/His122/Lys38 in RNase6 corresponding to His12/His119/Lys41 in RNaseA). Recently, our first crystal structure of human RNase6 identified an additional His pair (His36/His39) and suggested the presence of a secondary active site. PubMed: 30287244 DOI: 10.1016/j.bbagen.2018.09.021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation