5OGH

Structure of RNase A at high resolution (1.16 A) in complex with 3'-CMP and sulphate ions

Summary for 5OGH

Entry DOI	10.2210/pdb5ogh/pdb
Descriptor	Ribonuclease pancreatic, CYTIDINE-3'-MONOPHOSPHATE, SULFATE ION, ... (6 entities in total)
Functional Keywords	ribonuclease a, 3'-cmp, rnase a, mononucleotide inhibitor, high resolution, hydrolase
Biological source	Bos taurus (cattle)
Total number of polymer chains	1
Total formula weight	14674.03
Authors	Blanco, J.A.,Prats-Ejarque, G.,Salazar, V.A.,Moussaoui, M.,Boix, E. (deposition date: 2017-07-13, 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 (1.16 Å)

Structure validation