5OAB

A novel crystal form of human RNase6 at atomic resolution

Summary for 5OAB

Entry DOI	10.2210/pdb5oab/pdb
Related	4X09
Descriptor	Ribonuclease K6, PHOSPHATE ION, SODIUM ION, ... (6 entities in total)
Functional Keywords	rnase k6, hydrolase, pancreatic ribonuclease
Biological source	Homo sapiens (Human)
Total number of polymer chains	1
Total formula weight	15591.32
Authors	Prats-Ejarque, G.,Moussaoui, M.,Boix, E. (deposition date: 2017-06-21, release date: 2018-08-01, 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 (1.111 Å)

Structure validation